Tag | Content |
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CPLM ID | CPLM-006320 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Heat shock protein 78, mitochondrial |
Protein Synonyms/Alias | |
Gene Name | HSP78 |
Gene Synonyms/Alias | YDR258C; YD9320A.08C |
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 |
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113 | TKLARDGKLDPVIGR | acetylation | [1] | 349 | SKPDEIQKLDRAIMK | acetylation | [1] | 366 | IELESLKKETDPVSV | acetylation | [1] | 474 | VTSDDISKVVAKMTG | acetylation | [1] | 576 | DMSEFQEKHTVSRLI | acetylation | [1] | 792 | RVVVKDTKLVVLPNH | acetylation | [1] |
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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] |
Functional Description | Required, in concert with mitochondrial Hsp70 (SSC1), for the dissociation, resolubilization and refolding of aggregates of damaged proteins in the mitochondrial matrix after heat stress. May extract proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by the Hsp70 chaperone system. Required for resumption of mitochondrial respiratory function, DNA synthesis and morphology after heat stress. Its main role may be maintaining the molecular chaperone SSC1 in a soluble and functional state. Also required for the efficient degradation of proteins by matrix protease PIM1, independent on its protein remodeling activity. |
Sequence Annotation | NP_BIND 143 150 ATP 1 (Potential). NP_BIND 541 548 ATP 2 (Potential). REGION 98 344 NBD1. REGION 467 658 NBD2. |
Keyword | ATP-binding; Chaperone; Coiled coil; Complete proteome; Direct protein sequencing; Mitochondrion; Nucleotide-binding; Reference proteome; Repeat; Stress response; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 811 AA |
Protein Sequence | MLRQATKAPI QKYLQRTQLL RRSTPRIYTI VQCKRSICSF NARPRVANKL LSDIKTNALN 60 EVAISTCALK SSYGLPNFKR TYVQMRMDPN QQPEKPALEQ FGTNLTKLAR DGKLDPVIGR 120 DEEIARAIQI LSRRTKNNPC LIGRAGVGKT ALIDGLAQRI VAGEVPDSLK DKDLVALDLG 180 SLIAGAKYRG EFEERLKKVL EEIDKANGKV IVFIDEVHML LGLGKTDGSM DASNILKPKL 240 ARGLRCISAT TLDEFKIIEK DPALSRRFQP ILLNEPSVSD TISILRGLKE RYEVHHGVRI 300 TDTALVSAAV LSNRYITDRF LPDKAIDLVD EACAVLRLQH ESKPDEIQKL DRAIMKIQIE 360 LESLKKETDP VSVERREALE KDLEMKNDEL NRLTKIWDAE RAEIESIKNA KANLEQARIE 420 LEKCQREGDY TKASELRYSR IPDLEKKVAL SEKSKDGDKV NLLHDSVTSD DISKVVAKMT 480 GIPTETVMKG DKDRLLYMEN SLKERVVGQD EAIAAISDAV RLQRAGLTSE KRPIASFMFL 540 GPTGTGKTEL TKALAEFLFD DESNVIRFDM SEFQEKHTVS RLIGAPPGYV LSESGGQLTE 600 AVRRKPYAVV LFDEFEKAHP DVSKLLLQVL DEGKLTDSLG HHVDFRNTII VMTSNIGQDI 660 LLNDTKLGDD GKIDTATKNK VIEAMKRSYP PEFINRIDDI LVFNRLSKKV LRSIVDIRIA 720 EIQDRLAEKR MKIDLTDEAK DWLTDKGYDQ LYGARPLNRL IHRQILNSMA TFLLKGQIRN 780 GETVRVVVKD TKLVVLPNHE EGEVVEEEAE K 811 |
Gene Ontology | GO:0005759; C:mitochondrial matrix; IDA:SGD. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0016887; F:ATPase activity; IDA:SGD. GO:0051787; F:misfolded protein binding; IDA:SGD. GO:0034605; P:cellular response to heat; IMP:SGD. GO:0000002; P:mitochondrial genome maintenance; IGI:SGD. GO:0010892; P:positive regulation of mitochondrial translation in response to stress; IMP:SGD. GO:0030150; P:protein import into mitochondrial matrix; IGI:SGD. GO:0042026; P:protein refolding; IDA:SGD. GO:0050821; P:protein stabilization; IMP:SGD. GO:0043335; P:protein unfolding; IMP:SGD. |
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