HSP82/YPL240C Protein Information Help

Standard Name Hsp82p 1, 2
Systematic Name Ypl240cp
Alias Hsp90p 3
ORF Classification Verified
Description Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication (10, 11, 12, 13, 4, 5, 6, 7, 8, 9)
Name Description Heat Shock Protein 14
Experimental Data
Molecules/cell 445000 15
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 709
Molecular Weight (Da) 81,406
Isoelectric Point (pI) 4.66

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Hsp82p (InterPro)
Physical Interactions There are 528 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000053297 | P02829
MIPS: YPL240C
NCBI: 1061249 | 110590736 | 110590737 | 119389067 | 119390310 | 119390313 | 119390314 | 123677 | 126030488 | 1370495 | 157829682 | 157829876 | 157829955 | 157829974 | 157830302 | 171725 | 193506614 | 194709140 | 194709141 | 197724987 | 197724988 | 197724989 | 197724990 | 226887606 | 226887607 | 226887609 | 226887610 | 254839283 | 2624655 | 2624656 | 302565956 | 357380333 | 357380334 | 357380335 | 357380336 | 357380337 | 357380338 | 357380343 | 357380344 | 357380345 | 42542979 | 42542980 | 42543754 | 42543756 | 42543758 | 42543760 | 42543762 | 42543764 | 6325016 | 78101629 | 78101630 | 78101631 | 88192077 | 88192078 | 99031945 | 99031946 | 99031949 | 99031950 | 99031951 | NP_015084.1
GenBank/EMBL/DDBJ: DAA11197.1 | K01387 | Z67751 | Z73596
Amino Acid Sequence (or in FASTA format)
       1  MASETFEFQA EITQLMSLII NTVYSNKEIF LRELISNASD ALDKIRYKSL
      51  SDPKQLETEP DLFIRITPKP EQKVLEIRDS GIGMTKAELI NNLGTIAKSG
     101  TKAFMEALSA GADVSMIGQF GVGFYSLFLV ADRVQVISKS NDDEQYIWES
     151  NAGGSFTVTL DEVNERIGRG TILRLFLKDD QLEYLEEKRI KEVIKRHSEF
     201  VAYPIQLVVT KEVEKEVPIP EEEKKDEEKK DEEKKDEDDK KPKLEEVDEE
     251  EEKKPKTKKV KEEVQEIEEL NKTKPLWTRN PSDITQEEYN AFYKSISNDW
     301  EDPLYVKHFS VEGQLEFRAI LFIPKRAPFD LFESKKKKNN IKLYVRRVFI
     351  TDEAEDLIPE WLSFVKGVVD SEDLPLNLSR EMLQQNKIMK VIRKNIVKKL
     401  IEAFNEIAED SEQFEKFYSA FSKNIKLGVH EDTQNRAALA KLLRYNSTKS
     451  VDELTSLTDY VTRMPEHQKN IYYITGESLK AVEKSPFLDA LKAKNFEVLF
     501  LTDPIDEYAF TQLKEFEGKT LVDITKDFEL EETDEEKAER EKEIKEYEPL
     551  TKALKEILGD QVEKVVVSYK LLDAPAAIRT GQFGWSANME RIMKAQALRD
     601  SSMSSYMSSK KTFEISPKSP IIKELKKRVD EGGAQDKTVK DLTKLLYETA
     651  LLTSGFSLDE PTSFASRINR LISLGLNIDE DEETETAPEA STAAPVEEVP
     701  ADTEMEEVD*                                            

external links for Hsp82p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
YGOB BioPIXIE MIPS YeastGFP
YOGY CYC2008 (complexes) Pfam domains YeastRC Public Image Repository

Complexome YeastRC Structure Prediction (Seattle)

DIP


GeneMANIA


YeastRC Mass Spec (Seattle)

References cited on this page View Complete Literature Guide for Hsp82p
1) Stearns, T. and Botstein, D.  (1989) Personal Communication, Mortimer Map Edition 10
2) Gross, D.S.  (1992) Personal Communication, Mortimer Map Edition 11
3) Gross DS, et al.  (1990) Promoter function and in situ protein/DNA interactions upstream of the yeast HSP90 heat shock genes. Antonie Van Leeuwenhoek 58(3):175-86
4) Dolinski KJ, et al.  (1998) CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90. Mol Cell Biol 18(12):7344-52
5) Marsh JA, et al.  (1998) Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cells. Mol Cell Biol 18(12):7353-9
6) Duina AA, et al.  (1998) Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response. J Biol Chem 273(30):18974-8
7) Louvion JF, et al.  (1998) Hsp90 is required for pheromone signaling in yeast. Mol Biol Cell 9(11):3071-83
8) Prodromou C, et al.  (1999) Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones. EMBO J 18(3):754-62
9) Young JC, et al.  (2003) Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112(1):41-50
10) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
11) Toogun OA, et al.  (2008) The hsp90 molecular chaperone modulates multiple telomerase activities. Mol Cell Biol 28(1):457-67
12) Pursell NW, et al.  (2012) Solubility-promoting function of Hsp90 contributes to client maturation and robust cell growth. Eukaryot Cell 11(8):1033-41
13) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
14) Finkelstein DB and Strausberg S  (1983) Identification and expression of a cloned yeast heat shock gene. J Biol Chem 258(3):1908-13
15) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41