HSP78/YDR258C Protein Information Help

Standard Name Hsp78p
Systematic Name Ydr258cp
ORF Classification Verified
Description Oligomeric mitochondrial matrix chaperone that cooperates with Ssc1p in mitochondrial thermotolerance after heat shock; able to prevent the aggregation of misfolded proteins as well as resolubilize protein aggregates (1, 2, 3, 4, 5, 6, 7)
Name Description Heat Shock Protein 2
Experimental Data
Molecules/cell 2990 8
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 811
Molecular Weight (Da) 91,335
Isoelectric Point (pI) 8.13

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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 Hsp78p (InterPro)
Physical Interactions There are 48 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000006A281 | P33416
MIPS: YDR258C
NCBI: 1136213 | 1226034 | 31077173 | 388369 | 398366295 | NP_010544.3
GenBank/EMBL/DDBJ: DAA12098.1 | L16533 | Z68329 | Z70202
Amino Acid Sequence (or in FASTA format)
 
       1  MLRQATKAPI QKYLQRTQLL RRSTPRIYTI VQCKRSICSF NARPRVANKL
      51  LSDIKTNALN EVAISTCALK SSYGLPNFKR TYVQMRMDPN QQPEKPALEQ
     101  FGTNLTKLAR DGKLDPVIGR DEEIARAIQI LSRRTKNNPC LIGRAGVGKT
     151  ALIDGLAQRI VAGEVPDSLK DKDLVALDLG SLIAGAKYRG EFEERLKKVL
     201  EEIDKANGKV IVFIDEVHML LGLGKTDGSM DASNILKPKL ARGLRCISAT
     251  TLDEFKIIEK DPALSRRFQP ILLNEPSVSD TISILRGLKE RYEVHHGVRI
     301  TDTALVSAAV LSNRYITDRF LPDKAIDLVD EACAVLRLQH ESKPDEIQKL
     351  DRAIMKIQIE LESLKKETDP VSVERREALE KDLEMKNDEL NRLTKIWDAE
     401  RAEIESIKNA KANLEQARIE LEKCQREGDY TKASELRYSR IPDLEKKVAL
     451  SEKSKDGDKV NLLHDSVTSD DISKVVAKMT GIPTETVMKG DKDRLLYMEN
     501  SLKERVVGQD EAIAAISDAV RLQRAGLTSE KRPIASFMFL GPTGTGKTEL
     551  TKALAEFLFD DESNVIRFDM SEFQEKHTVS RLIGAPPGYV LSESGGQLTE
     601  AVRRKPYAVV LFDEFEKAHP DVSKLLLQVL DEGKLTDSLG HHVDFRNTII
     651  VMTSNIGQDI LLNDTKLGDD GKIDTATKNK VIEAMKRSYP PEFINRIDDI
     701  LVFNRLSKKV LRSIVDIRIA EIQDRLAEKR MKIDLTDEAK DWLTDKGYDQ
     751  LYGARPLNRL IHRQILNSMA TFLLKGQIRN GETVRVVVKD TKLVVLPNHE
     801  EGEVVEEEAE K*

external links for Hsp78p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Candida (CGD) BioPIXIE MIPS YeastRC Public Image Repository
Candida (CandidaDB) CYC2008 (complexes) Pfam domains
YGOB Complexome YeastRC Structure Prediction (Seattle)
YOGY GeneMANIA


YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Hsp78p
1) Schmitt M, et al.  (1995) Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. EMBO J 14(14):3434-44
2) Leonhardt SA, et al.  (1993) HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Mol Cell Biol 13(10):6304-13
3) Moczko M, et al.  (1995) The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function. J Mol Biol 254(4):538-43
4) Schmitt M, et al.  (1996) The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria. J Cell Biol 134(6):1375-86
5) Germaniuk A, et al.  (2002) A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase. J Biol Chem 277(31):27801-8
6) Rottgers K, et al.  (2002) The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix. J Biol Chem 277(48):45829-37
7) von Janowsky B, et al.  (2006) The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress. J Mol Biol 357(3):793-807
8) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41