UniProt Accession

 HSP82_YEAST; P02829; D6W3D1 

Genbank Protein ID

 K01387; Z67751; Z73596; BK006949 

Genbank Nucleotide ID

 AAA02743.1; CAA91604.1; CAA97961.1; DAA11197.1 

Protein Name

 ATP-dependent molecular chaperone HSP82 

Protein Synonyms/Alias

 82 kDa heat shock protein; Heat shock protein Hsp90 heat-inducible isoform 

Gene Name

 HSP82 

Gene Synonyms/Alias

 HSP90; YPL240C 

Created Date

 July 27, 2013 

Organism

 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 

NCBI Taxa ID

 559292 

Lysine Modification

Position	Peptide	Type	References
44	NASDALDKIRYKSLS	acetylation	[1]
44	NASDALDKIRYKSLS	ubiquitination	[2]
54	YKSLSDPKQLETEPD	acetylation	[1]
54	YKSLSDPKQLETEPD	ubiquitination	[2]
69	LFIRITPKPEQKVLE	ubiquitination	[2]
86	DSGIGMTKAELINNL	acetylation	[1]
86	DSGIGMTKAELINNL	ubiquitination	[2]
98	NNLGTIAKSGTKAFM	ubiquitination	[2]
178	TILRLFLKDDQLEYL	acetylation	[1]
178	TILRLFLKDDQLEYL	ubiquitination	[2]
188	QLEYLEEKRIKEVIK	acetylation	[1]
211	PIQLVVTKEVEKEVP	ubiquitination	[3]
215	VVTKEVEKEVPIPEE	acetylation	[1]
224	VPIPEEEKKDEEKKD	acetylation	[1]
253	EVDEEEEKKPKTKKV	acetylation	[1]
274	IEELNKTKPLWTRNP	ubiquitination	[2]
294	EEYNAFYKSISNDWE	ubiquitination	[2]
307	WEDPLYVKHFSVEGQ	ubiquitination	[2]
325	RAILFIPKRAPFDLF	acetylation	[1]
325	RAILFIPKRAPFDLF	ubiquitination	[2]
342	KKKKNNIKLYVRRVF	acetylation	[1]
342	KKKKNNIKLYVRRVF	ubiquitination	[2]
387	REMLQQNKIMKVIRK	acetylation	[1]
387	REMLQQNKIMKVIRK	ubiquitination	[2]
399	IRKNIVKKLIEAFNE	acetylation	[1]
416	EDSEQFEKFYSAFSK	ubiquitination	[2]
423	KFYSAFSKNIKLGVH	acetylation	[1]
426	SAFSKNIKLGVHEDT	acetylation	[1]
426	SAFSKNIKLGVHEDT	ubiquitination	[2]
441	QNRAALAKLLRYNST	acetylation	[1]
441	QNRAALAKLLRYNST	ubiquitination	[2]
449	LLRYNSTKSVDELTS	acetylation	[1]
449	LLRYNSTKSVDELTS	ubiquitination	[2]
469	TRMPEHQKNIYYITG	acetylation	[1]
480	YITGESLKAVEKSPF	acetylation	[1]
484	ESLKAVEKSPFLDAL	acetylation	[1]
484	ESLKAVEKSPFLDAL	ubiquitination	[2]
492	SPFLDALKAKNFEVL	acetylation	[1]
492	SPFLDALKAKNFEVL	ubiquitination	[2]
519	QLKEFEGKTLVDITK	acetylation	[1]
519	QLKEFEGKTLVDITK	ubiquitination	[2]
537	LEETDEEKAEREKEI	acetylation	[1]
545	AEREKEIKEYEPLTK	acetylation	[1]
545	AEREKEIKEYEPLTK	ubiquitination	[2]
552	KEYEPLTKALKEILG	acetylation	[1]
552	KEYEPLTKALKEILG	ubiquitination	[2]
555	EPLTKALKEILGDQV	ubiquitination	[2]
570	EKVVVSYKLLDAPAA	acetylation	[1]
570	EKVVVSYKLLDAPAA	ubiquitination	[2]
594	ANMERIMKAQALRDS	ubiquitination	[2]
610	MSSYMSSKKTFEISP	ubiquitination	[2]
611	SSYMSSKKTFEISPK	ubiquitination	[2]
618	KTFEISPKSPIIKEL	acetylation	[1]
618	KTFEISPKSPIIKEL	ubiquitination	[2]
623	SPKSPIIKELKKRVD	acetylation	[1]
623	SPKSPIIKELKKRVD	ubiquitination	[2]
637	DEGGAQDKTVKDLTK	acetylation	[1]
637	DEGGAQDKTVKDLTK	ubiquitination	[2]

Reference

 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [3] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047] 

Functional Description

 Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures. 

Sequence Annotation

 REPEAT 221 225 1.
 REPEAT 226 230 2.
 REPEAT 231 235 3.
 REPEAT 237 241 4.
 REPEAT 250 254 5.
 REGION 221 263 5 X 5 AA repeats of [DE]-[DE]-[DE]-K-K;
 MOTIF 705 709 TPR repeat-binding.
 BINDING 37 37 ATP.
 BINDING 79 79 ATP.
 BINDING 98 98 ATP.
 BINDING 124 124 ATP; via amide nitrogen.
 BINDING 380 380 ATP.
 MOD_RES 657 657 Phosphoserine (By similarity).  

Keyword

 3D-structure; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Stress response. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 709 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0042623; F:ATPase activity, coupled; IDA:SGD.
 GO:0051082; F:unfolded protein binding; IDA:SGD.
 GO:0006458; P:'de novo' protein folding; IDA:SGD.
 GO:0000492; P:box C/D snoRNP assembly; IMP:SGD.
 GO:0032212; P:positive regulation of telomere maintenance via telomerase; IPI:SGD.
 GO:0043248; P:proteasome assembly; IGI:SGD.
 GO:0042026; P:protein refolding; IMP:SGD.
 GO:0006626; P:protein targeting to mitochondrion; IPI:SGD.
 GO:0006970; P:response to osmotic stress; IMP:SGD. 

Interpro

 IPR003594; HATPase_ATP-bd.
 IPR019805; Heat_shock_protein_90_CS.
 IPR001404; Hsp90.
 IPR020575; Hsp90_N.
 IPR020568; Ribosomal_S5_D2-typ_fold. 

Pfam

 PF02518; HATPase_c
 PF00183; HSP90 

SMART

 SM00387; HATPase_c 

PROSITE

 PS00298; HSP90 

PRINTS

 PR00775; HEATSHOCK90.