HSP78_YEAST - dbPTM
HSP78_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSP78_YEAST
UniProt AC P33416
Protein Name Heat shock protein 78, mitochondrial
Gene Name HSP78
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 811
Subcellular Localization Mitochondrion matrix .
Protein 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..
Protein Sequence MLRQATKAPIQKYLQRTQLLRRSTPRIYTIVQCKRSICSFNARPRVANKLLSDIKTNALNEVAISTCALKSSYGLPNFKRTYVQMRMDPNQQPEKPALEQFGTNLTKLARDGKLDPVIGRDEEIARAIQILSRRTKNNPCLIGRAGVGKTALIDGLAQRIVAGEVPDSLKDKDLVALDLGSLIAGAKYRGEFEERLKKVLEEIDKANGKVIVFIDEVHMLLGLGKTDGSMDASNILKPKLARGLRCISATTLDEFKIIEKDPALSRRFQPILLNEPSVSDTISILRGLKERYEVHHGVRITDTALVSAAVLSNRYITDRFLPDKAIDLVDEACAVLRLQHESKPDEIQKLDRAIMKIQIELESLKKETDPVSVERREALEKDLEMKNDELNRLTKIWDAERAEIESIKNAKANLEQARIELEKCQREGDYTKASELRYSRIPDLEKKVALSEKSKDGDKVNLLHDSVTSDDISKVVAKMTGIPTETVMKGDKDRLLYMENSLKERVVGQDEAIAAISDAVRLQRAGLTSEKRPIASFMFLGPTGTGKTELTKALAEFLFDDESNVIRFDMSEFQEKHTVSRLIGAPPGYVLSESGGQLTEAVRRKPYAVVLFDEFEKAHPDVSKLLLQVLDEGKLTDSLGHHVDFRNTIIVMTSNIGQDILLNDTKLGDDGKIDTATKNKVIEAMKRSYPPEFINRIDDILVFNRLSKKVLRSIVDIRIAEIQDRLAEKRMKIDLTDEAKDWLTDKGYDQLYGARPLNRLIHRQILNSMATFLLKGQIRNGETVRVVVKDTKLVVLPNHEEGEVVEEEAEK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
95AcetylationDPNQQPEKPALEQFG
CCCCCCCCHHHHHHC		42.1224489116
107AcetylationQFGTNLTKLARDGKL
HHCCHHHHHHCCCCC		43.2324489116
113AcetylationTKLARDGKLDPVIGR
HHHHCCCCCCCCCCC		54.7424489116
149UbiquitinationIGRAGVGKTALIDGL
ECCCCCCHHHHHHHH		28.3724961812
170AcetylationGEVPDSLKDKDLVAL
CCCCCCCCCCCEEEE		67.6824489116
172AcetylationVPDSLKDKDLVALDL
CCCCCCCCCEEEEEH		51.9124489116
187AcetylationGSLIAGAKYRGEFEE
HHHHHCHHCCCHHHH		34.2624489116
205AcetylationKVLEEIDKANGKVIV
HHHHHHHHHCCEEEE		49.7925381059
237AcetylationMDASNILKPKLARGL
CCHHHCCCHHHHHCC		35.9924489116
239AcetylationASNILKPKLARGLRC
HHHCCCHHHHHCCEE		53.8724489116
251PhosphorylationLRCISATTLDEFKII
CEEEEECCHHHEEEE		31.7428889911
260AcetylationDEFKIIEKDPALSRR
HHEEEEECCHHHHHC		59.6124489116
277PhosphorylationPILLNEPSVSDTISI
CEECCCCCHHHHHHH		28.2422369663
279PhosphorylationLLNEPSVSDTISILR
ECCCCCHHHHHHHHH		33.1122369663
281PhosphorylationNEPSVSDTISILRGL
CCCCHHHHHHHHHHH		14.7622369663
283PhosphorylationPSVSDTISILRGLKE
CCHHHHHHHHHHHHH		20.0522369663
349AcetylationSKPDEIQKLDRAIMK
CCHHHHHHHHHHHHH		59.0022865919
366AcetylationIELESLKKETDPVSV
HHHHHHCCCCCCCCH		71.7524489116
372PhosphorylationKKETDPVSVERREAL
CCCCCCCCHHHHHHH		24.5330377154
381AcetylationERREALEKDLEMKND
HHHHHHHHHHHHCHH		69.3424489116
386AcetylationLEKDLEMKNDELNRL
HHHHHHHCHHHHHHH		52.4524489116
395AcetylationDELNRLTKIWDAERA
HHHHHHHHHHHHHHH		46.5224489116
406PhosphorylationAERAEIESIKNAKAN
HHHHHHHHHHHHHHH		44.5227214570
408AcetylationRAEIESIKNAKANLE
HHHHHHHHHHHHHHH		61.2025381059
454PhosphorylationKVALSEKSKDGDKVN
HHHHCCCCCCCCCEE		31.7423607784
466PhosphorylationKVNLLHDSVTSDDIS
CEECCCCCCCHHHHH		19.2923607784
468PhosphorylationNLLHDSVTSDDISKV
ECCCCCCCHHHHHHH		30.3223607784
469PhosphorylationLLHDSVTSDDISKVV
CCCCCCCHHHHHHHH		31.0023607784
473PhosphorylationSVTSDDISKVVAKMT
CCCHHHHHHHHHHHH		26.7923607784
474AcetylationVTSDDISKVVAKMTG
CCHHHHHHHHHHHHC		40.8524489116
480PhosphorylationSKVVAKMTGIPTETV
HHHHHHHHCCCHHHH		31.1122369663
484PhosphorylationAKMTGIPTETVMKGD
HHHHCCCHHHHCCCC		42.2222369663
486PhosphorylationMTGIPTETVMKGDKD
HHCCCHHHHCCCCHH		28.5122369663
531AcetylationRAGLTSEKRPIASFM
HCCCCCCCCCCEEEE		64.3424489116
576AcetylationDMSEFQEKHTVSRLI
EHHHHHHHHCHHHHH		33.5224489116
589PhosphorylationLIGAPPGYVLSESGG
HHCCCCCEEEECCCC		12.1822369663
592PhosphorylationAPPGYVLSESGGQLT
CCCCEEEECCCCCCC		21.4822369663
594PhosphorylationPGYVLSESGGQLTEA
CCEEEECCCCCCCHH		44.8622369663
599PhosphorylationSESGGQLTEAVRRKP
ECCCCCCCHHHHHCC		17.6322369663
746AcetylationAKDWLTDKGYDQLYG
HHHHHHHCCHHHHCC		54.8824489116
789SuccinylationETVRVVVKDTKLVVL
CEEEEEEECCEEEEC		48.3323954790
792AcetylationRVVVKDTKLVVLPNH
EEEEECCEEEECCCC		49.7924489116
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of HSP78_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSP78_YEAST !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of HSP78_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP77_YEASTSSC1genetic
7628444
UBP3_YEASTUBP3physical
19536198
TFS2_YEASTDST1physical
19536198
PRS8_YEASTRPT6physical
19536198
MDS3_YEASTMDS3physical
19536198
SYV_YEASTVAS1physical
19536198
PFKA1_YEASTPFK1physical
19536198
MYO1_YEASTMYO1physical
19536198
PRP8_YEASTPRP8physical
19536198
RSC4_YEASTRSC4physical
19536198
METK1_YEASTSAM1physical
19536198
SKG3_YEASTSKG3physical
19536198
CSR1_YEASTCSR1physical
19536198
CDC73_YEASTCDC73physical
19536198
ECM5_YEASTECM5physical
19536198
PRS6A_YEASTRPT5physical
19536198
MYO2_YEASTMYO2physical
19536198
SPP1_YEASTSPP1physical
19536198
NAB3_YEASTNAB3physical
19536198
SSB1_YEASTSSB1physical
19536198
MBA1_YEASTMBA1genetic
20093466
MED5_YEASTNUT1genetic
20093466
APQ12_YEASTAPQ12genetic
20093466
FMS1_YEASTFMS1genetic
20093466
MED9_YEASTCSE2genetic
20093466
ARE2_YEASTARE2genetic
20093466
COS10_YEASTCOS10genetic
20093466
LEU9_YEASTLEU9genetic
20093466
RTC5_YEASTRTC5genetic
20093466
DCS2_YEASTDCS2genetic
20093466
MSS18_YEASTMSS18genetic
20093466
MBA1_YEASTMBA1genetic
27708008
SNT1_YEASTSNT1genetic
27708008
IMG2_YEASTIMG2genetic
27708008
PT122_YEASTPET122genetic
27708008
MED5_YEASTNUT1genetic
27708008
CSK2C_YEASTCKB2genetic
27708008
DIA2_YEASTDIA2genetic
27708008
LEU9_YEASTLEU9genetic
27708008
SFL1_YEASTSFL1genetic
27708008
DCS2_YEASTDCS2genetic
27708008
MED1_YEASTMED1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSP78_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, AND MASSSPECTROMETRY.

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