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Sample Preparation and Post-separation Analysis Searching in 'SWISS-2DPAGE' for entry matching: P02829 SWISS-2DPAGE:  P02829 P02829 General information about the entry View entry in simple text format Entry name HSP82_YEAST Primary accession number P02829 integrated into SWISS-2DPAGE on  August 1, 1995 (release 2) 2D Annotations were last modified on October 1, 2001 (version 1) General Annotations were last modified on  May 19, 2011 (version 11) Name and origin of the protein Description RecName: Full=ATP-dependent molecular chaperone HSP82; AltName: Full=82 kDa heat shock protein; AltName: Full=Heat shock protein Hsp90 heat-inducible isoform;. Gene name Name=HSP82 Synonyms=HSP90 OrderedLocusNames=YPL240C Annotated species Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. References [1]   MAPPING ON GEL MEDLINE=96314060; PubMed=8740180; [NCBI, Expasy, EBI, Israel, Japan] Sanchez J.-C., Golaz O., Frutiger S., Schaller D., Appel R.D., Bairoch A., Hughes G.J., Hochstrasser D.F. ''''''The yeast SWISS-2DPAGE database'';'';'' Electrophoresis 17(1):556-565(1996) [2]   MAPPING ON GEL MEDLINE=95203288; PubMed=7895733; [NCBI, Expasy, EBI, Israel, Japan] Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S. ''''''Protein identifications for a Saccharomyces cerevisiae protein database'';'';'' Electrophoresis 15(1):1466-1486(1994) Comments SUBUNIT: MONOMER 2D PAGE maps for identified proteins How to interpret a protein YEAST {Saccharomyces cerevisiae} Saccharomyces cerevisiae (Baker's yeast)   map experimental info   protein estimated location   YEAST MAP LOCATIONS: SPOT 2D-000IRA: pI=4.78; Mw=88619 MAPPING (identification): GEL MATCHING [1] AND IDENTIFIED BY GARRELS [2]. Copyright This SWISS-2DPAGE entry is copyright the Swiss Institute of Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified and this statement is not removed. Usage by and for commercial entities requires a license agreement (See http://world-2dpage.expasy.org/swiss-2dpage/docs/license.html or send email from legal@sib.swiss). Cross-references UniProtKB/Swiss-Prot P02829; HSP82_YEAST. YEPD 9884. YEPD 9908. 2D PAGE maps for identified proteins How to interpret a protein map You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw. Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly. Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed. External data extracted from UniProtKB/Swiss-Prot Extracted from UniProtKB/Swiss-Prot, release: 2011_10 Entry name HSP82_YEAST Primary accession number P02829 Secondary accession number(s) D6W3D1 Sequence was last modified on  July 21, 1986 (version 1) Annotations were last modified on  October 19, 2011 (version 136) Name and origin of the protein Description RecName: Full=ATP-dependent molecular chaperone HSP82; AltName: Full=82 kDa heat shock protein; AltName: Full=Heat shock protein Hsp90 heat-inducible isoform; Gene name Name=HSP82 Synonyms=HSP90 OrderedLocusNames=YPL240C Encoded on Name=HSP82; Synonyms=HSP90; OrderedLocusNames=YPL240C Keywords 3D-structure; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Stress response. Copyright Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL K01387; AAA02743.1; -; Unassigned_RNA EMBL Z67751; CAA91604.1; -; Genomic_DNA EMBL Z73596; CAA97961.1; -; Genomic_DNA EMBL BK006949; DAA11197.1; -; Genomic_DNA PIR A03313; HHBY90; . RefSeq NP_015084.1; NM_001184054.1; . PDB 1A4H; X-ray; 2.50 A; A=1-220 PDB 1AH6; X-ray; 1.80 A; A=1-220 PDB 1AH8; X-ray; 2.10 A; A/B=1-220 PDB 1AM1; X-ray; 2.00 A; A=2-214 PDB 1AMW; X-ray; 1.85 A; A=1-214 PDB 1BGQ; X-ray; 2.50 A; A=1-214 PDB 1HK7; X-ray; 2.50 A; A/B=273-560 PDB 1US7; X-ray; 2.30 A; A=1-214 PDB 1USU; X-ray; 2.15 A; A=273-530 PDB 1USV; X-ray; 2.70 A; A/C/E/G=272-530 PDB 1ZW9; X-ray; 1.90 A; A=1-220 PDB 1ZWH; X-ray; 1.65 A; A=1-220 PDB 2AKP; X-ray; 1.94 A; A/B=25-210 PDB 2BRC; X-ray; 1.60 A; A=1-214 PDB 2BRE; X-ray; 2.00 A; A/B=1-219 PDB 2CG9; X-ray; 3.10 A; A/B=1-677 PDB 2CGE; X-ray; 3.00 A; A/B/D=273-677 PDB 2CGF; X-ray; 2.20 A; A=1-214 PDB 2FXS; X-ray; 2.00 A; A=1-220 PDB 2IWS; X-ray; 2.70 A; A=1-214 PDB 2IWU; X-ray; 2.80 A; A=1-214 PDB 2IWX; X-ray; 1.50 A; A=1-214 PDB 2VW5; X-ray; 1.90 A; A/B/C/D=1-214 PDB 2VWC; X-ray; 2.40 A; A=1-219 PDB 2WEP; X-ray; 2.00 A; A=1-220 PDB 2WEQ; X-ray; 2.20 A; A=1-220 PDB 2WER; X-ray; 1.60 A; A/B=1-220 PDB 2XD6; X-ray; 2.20 A; A=1-214 PDB 3C0E; X-ray; 1.90 A; A=1-220 PDB 3C11; X-ray; 1.60 A; A=1-220 PDB 3FP2; X-ray; 1.98 A; Q=698-709 PDBsum 1A4H; -; . PDBsum 1AH6; -; . PDBsum 1AH8; -; . PDBsum 1AM1; -; . PDBsum 1AMW; -; . PDBsum 1BGQ; -; . PDBsum 1HK7; -; . PDBsum 1US7; -; . PDBsum 1USU; -; . PDBsum 1USV; -; . PDBsum 1ZW9; -; . PDBsum 1ZWH; -; . PDBsum 2AKP; -; . PDBsum 2BRC; -; . PDBsum 2BRE; -; . PDBsum 2CG9; -; . PDBsum 2CGE; -; . PDBsum 2CGF; -; . PDBsum 2FXS; -; . PDBsum 2IWS; -; . PDBsum 2IWU; -; . PDBsum 2IWX; -; . PDBsum 2VW5; -; . PDBsum 2VWC; -; . PDBsum 2WEP; -; . PDBsum 2WEQ; -; . PDBsum 2WER; -; . PDBsum 2XD6; -; . PDBsum 3C0E; -; . PDBsum 3C11; -; . PDBsum 3FP2; -; . ProteinModelPortal P02829; -; . SMR P02829; 1-677; . DIP DIP-2262N; -; . IntAct P02829; 325; . MINT MINT-560200; -; . STRING P02829; -; . SWISS-2DPAGE P02829; -; . PeptideAtlas P02829; -; . PRIDE P02829; -; . EnsemblFungi YPL240C; YPL240C; YPL240C; . GeneID 855836; -; . KEGG sce:YPL240C; -; . NMPDR fig|4932.3.peg.6211; -; . CYGD YPL240c; -; . SGD S000006161; HSP82; . eggNOG fuNOG05217; -; . GeneTree EFGT00050000005875; -; . HOGENOM HBG631012; -; . OMA GFSKNIK; -; . OrthoDB EOG4643M4; -; . PhylomeDB P02829; -; . NextBio 980407; -; . ArrayExpress P02829; -; . Genevestigator P02829; -; . GermOnline YPL240C; Saccharomyces cerevisiae; . GO GO:0005737; C:cytoplasm; IDA:SGD; . GO GO:0005524; F:ATP binding; IEA:UniProtKB-KW; . GO GO:0042623; F:ATPase activity; coupled; IDA:SGD GO GO:0051082; F:unfolded protein binding; IDA:SGD; . GO GO:0006458; P:'de novo' protein folding; IDA:SGD; . GO GO:0032212; P:positive regulation of telomere maintenance via telomerase; IDA:SGD; . GO GO:0043248; P:proteasome assembly; IGI:SGD; . GO GO:0042026; P:protein refolding; IMP:SGD; . GO GO:0006626; P:protein targeting to mitochondrion; IPI:SGD; . GO GO:0006970; P:response to osmotic stress; IMP:SGD; . InterPro IPR003594; ATPase-like_ATP-bd; . InterPro IPR019805; Heat_shock_protein_90_CS; . InterPro IPR001404; Hsp90; . InterPro IPR020575; Hsp90_N; . InterPro IPR020568; Ribosomal_S5_D2-typ_fold; . Gene3D G3DSA:3.30.565.10; ATP_bd_ATPase; 2; . PANTHER PTHR11528; Hsp90; 1; . Pfam PF02518; HATPase_c; 1; . Pfam PF00183; HSP90; 1; . PIRSF PIRSF002583; Hsp90; 1; . PRINTS PR00775; HEATSHOCK90; . SMART SM00387; HATPase_c; 1; . SUPFAM SSF55874; ATP_bd_ATPase; 1; . SUPFAM SSF54211; Ribosomal_S5_D2-typ_fold; 1; . PROSITE PS00298; HSP90; 1; . SWISS-2DPAGE (search AC)