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Protein

Heat shock protein STI1

Gene

STI1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in mediating the heat shock response of some HSP70 genes. It is required for optimal growth of yeast cells at both low and high temperature.

GO - Molecular functioni

  • ATPase inhibitor activity Source: SGD
  • Hsp70 protein binding Source: SGD
  • Hsp90 protein binding Source: SGD
  • mRNA binding Source: SGD

GO - Biological processi

  • protein folding Source: SGD
  • protein localization Source: SGD
Complete GO annotation...

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciYEAST:G3O-33574-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein STI1
Gene namesi
Name:STI1
Ordered Locus Names:YOR027W
ORF Names:OR26.17
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR027W.
SGDiS000005553. STI1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 589589Heat shock protein STI1PRO_0000106341Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki99 – 99Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki168 – 168Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei227 – 2271PhosphoserineCombined sources
Cross-linki384 – 384Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP15705.

2D gel databases

SWISS-2DPAGEP15705.

PTM databases

iPTMnetiP15705.

Expressioni

Inductioni

By heat shock and canavanine.

Interactioni

Subunit structurei

Part of a larger complex that includes HSP70, HSP90, and immunophilins.

Binary interactionsi

WithEntry#Exp.IntActNotes
HSC82P151083EBI-18418,EBI-8666
HSP82P028299EBI-18418,EBI-8659

GO - Molecular functioni

  • Hsp70 protein binding Source: SGD
  • Hsp90 protein binding Source: SGD

Protein-protein interaction databases

BioGridi34430. 103 interactions.
DIPiDIP-2329N.
IntActiP15705. 17 interactions.
MINTiMINT-707004.

Structurei

Secondary structure

1
589
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi133 – 1375Combined sources
Beta strandi138 – 1403Combined sources
Helixi142 – 1476Combined sources
Helixi152 – 1565Combined sources
Helixi160 – 16910Combined sources
Helixi174 – 1774Combined sources
Turni178 – 1803Combined sources
Helixi182 – 19211Combined sources
Turni193 – 1964Combined sources
Helixi262 – 27413Combined sources
Helixi278 – 29114Combined sources
Helixi296 – 30712Combined sources
Helixi311 – 32717Combined sources
Helixi332 – 34817Combined sources
Helixi352 – 36514Combined sources
Helixi369 – 39022Combined sources
Helixi395 – 40814Combined sources
Helixi412 – 42514Combined sources
Helixi430 – 44213Combined sources
Helixi446 – 45914Combined sources
Helixi464 – 47613Combined sources
Helixi480 – 49819Combined sources
Turni499 – 5024Combined sources
Helixi503 – 51614Combined sources
Helixi527 – 53610Combined sources
Helixi538 – 5447Combined sources
Helixi548 – 55811Combined sources
Helixi560 – 5689Combined sources
Helixi570 – 58112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LLVNMR-A127-197[»]
2LLWNMR-A519-589[»]
3UPVX-ray1.60A395-518[»]
3UQ3X-ray2.60A262-515[»]
ProteinModelPortaliP15705.
SMRiP15705. Positions 4-197, 262-589.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati5 – 3834TPR 1Add
BLAST
Repeati40 – 7334TPR 2Add
BLAST
Repeati74 – 10734TPR 3Add
BLAST
Domaini138 – 17740STI1 1Add
BLAST
Repeati262 – 29534TPR 4Add
BLAST
Repeati297 – 32832TPR 5Add
BLAST
Repeati336 – 36934TPR 6Add
BLAST
Repeati396 – 42934TPR 7Add
BLAST
Repeati430 – 46334TPR 8Add
BLAST
Repeati465 – 49228TPR 9Add
BLAST
Domaini537 – 57640STI1 2Add
BLAST

Sequence similaritiesi

Contains 2 STI1 domains.Curated
Contains 9 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

GeneTreeiENSGT00840000129761.
HOGENOMiHOG000186562.
InParanoidiP15705.
KOiK09553.
OMAiPKTSEMM.
OrthoDBiEOG7GN2WM.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR006636. STI1_HS-bd.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00515. TPR_1. 2 hits.
PF13181. TPR_8. 2 hits.
[Graphical view]
SMARTiSM00727. STI1. 2 hits.
SM00028. TPR. 9 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 7 hits.
PS50293. TPR_REGION. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15705-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLTADEYKQ QGNAAFTAKD YDKAIELFTK AIEVSETPNH VLYSNRSACY
60 70 80 90 100
TSLKKFSDAL NDANECVKIN PSWSKGYNRL GAAHLGLGDL DEAESNYKKA
110 120 130 140 150
LELDASNKAA KEGLDQVHRT QQARQAQPDL GLTQLFADPN LIENLKKNPK
160 170 180 190 200
TSEMMKDPQL VAKLIGYKQN PQAIGQDLFT DPRLMTIMAT LMGVDLNMDD
210 220 230 240 250
INQSNSMPKE PETSKSTEQK KDAEPQSDST TSKENSSKAP QKEESKESEP
260 270 280 290 300
MEVDEDDSKI EADKEKAEGN KFYKARQFDE AIEHYNKAWE LHKDITYLNN
310 320 330 340 350
RAAAEYEKGE YETAISTLND AVEQGREMRA DYKVISKSFA RIGNAYHKLG
360 370 380 390 400
DLKKTIEYYQ KSLTEHRTAD ILTKLRNAEK ELKKAEAEAY VNPEKAEEAR
410 420 430 440 450
LEGKEYFTKS DWPNAVKAYT EMIKRAPEDA RGYSNRAAAL AKLMSFPEAI
460 470 480 490 500
ADCNKAIEKD PNFVRAYIRK ATAQIAVKEY ASALETLDAA RTKDAEVNNG
510 520 530 540 550
SSAREIDQLY YKASQQRFQP GTSNETPEET YQRAMKDPEV AAIMQDPVMQ
560 570 580
SILQQAQQNP AALQEHMKNP EVFKKIQTLI AAGIIRTGR
Length:589
Mass (Da):66,265
Last modified:April 1, 1990 - v1
Checksum:iCF8A85C2BBD3C44C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28486 Genomic DNA. Translation: AAA35121.1.
X87331 Genomic DNA. Translation: CAA60743.1.
Z74935 Genomic DNA. Translation: CAA99217.1.
BK006948 Genomic DNA. Translation: DAA10809.1.
PIRiA32567.
RefSeqiNP_014670.1. NM_001183446.1.

Genome annotation databases

EnsemblFungiiYOR027W; YOR027W; YOR027W.
GeneIDi854192.
KEGGisce:YOR027W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28486 Genomic DNA. Translation: AAA35121.1.
X87331 Genomic DNA. Translation: CAA60743.1.
Z74935 Genomic DNA. Translation: CAA99217.1.
BK006948 Genomic DNA. Translation: DAA10809.1.
PIRiA32567.
RefSeqiNP_014670.1. NM_001183446.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LLVNMR-A127-197[»]
2LLWNMR-A519-589[»]
3UPVX-ray1.60A395-518[»]
3UQ3X-ray2.60A262-515[»]
ProteinModelPortaliP15705.
SMRiP15705. Positions 4-197, 262-589.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34430. 103 interactions.
DIPiDIP-2329N.
IntActiP15705. 17 interactions.
MINTiMINT-707004.

PTM databases

iPTMnetiP15705.

2D gel databases

SWISS-2DPAGEP15705.

Proteomic databases

MaxQBiP15705.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR027W; YOR027W; YOR027W.
GeneIDi854192.
KEGGisce:YOR027W.

Organism-specific databases

EuPathDBiFungiDB:YOR027W.
SGDiS000005553. STI1.

Phylogenomic databases

GeneTreeiENSGT00840000129761.
HOGENOMiHOG000186562.
InParanoidiP15705.
KOiK09553.
OMAiPKTSEMM.
OrthoDBiEOG7GN2WM.

Enzyme and pathway databases

BioCyciYEAST:G3O-33574-MONOMER.

Miscellaneous databases

PROiP15705.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR006636. STI1_HS-bd.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00515. TPR_1. 2 hits.
PF13181. TPR_8. 2 hits.
[Graphical view]
SMARTiSM00727. STI1. 2 hits.
SM00028. TPR. 9 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 7 hits.
PS50293. TPR_REGION. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae."
    Nicolet C.M., Craig E.A.
    Mol. Cell. Biol. 9:3638-3646(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Snap helix with knob and hole: essential repeats in S. pombe nuclear protein nuc2+."
    Hirano T., Kinoshita N., Morikawa K., Yanagida M.
    Cell 60:319-328(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: PROTEIN SEQUENCE OF 76-93.
    Strain: ATCC 204508 / S288c.
  6. Cited for: DOMAINS TPR REPEATS.
  7. "Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70."
    Smith D.F., Sullivan W.P., Marion T.N., Zaitsu K., Madden B., McCormick D.J., Toft D.O.
    Mol. Cell. Biol. 13:869-876(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes."
    Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.
    Mol. Syst. Biol. 5:308-308(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].
  12. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-99; LYS-168 AND LYS-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSTI1_YEAST
AccessioniPrimary (citable) accession number: P15705
Secondary accession number(s): D6W293
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 6, 2016
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 67600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.