HSP60_SCHPO - dbPTM
HSP60_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSP60_SCHPO
UniProt AC Q09864
Protein Name Heat shock protein 60, mitochondrial
Gene Name hsp60
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 582
Subcellular Localization Mitochondrion.
Protein Description May participate in assembly and/or disassembly of proteins imported into the mitochondrion. HSP60 are ATPases and have affinity for unfolded proteins..
Protein Sequence MVSFLSSSVSRLPLRIAGRRIPGRFAVPQVRTYAKDLKFGVDARASLLTGVDTLARAVSVTLGPKGRNVLIDQPFGSPKITKDGVTVARSVSLKDKFENLGARLVQDVASKTNEVAGDGTTTATVLTRAIFSETVRNVAAGCNPMDLRRGIQLAVDNVVEFLQANKRDITTSEEISQVATISANGDTHIGELLAKAMERVGKEGVITVKEGRTISDELEVTEGMKFDRGYISPYFITDVKSQKVEFENPLILLSEKKVSAVQDILPSLELAAQQRRPLVIIAEDVDGEALAACILNKLRGQLQVVAIKAPGFGDNRRNMLGDLAVLTDSAVFNDEIDVSIEKAQPHHLGSCGSVTVTKEDTIIMKGAGDHVKVNDRCEQIRGVMADPNLTEYEKEKLQERLAKLSGGIAVIKVGGSSEVEVNEKKDRIVDALNAVKAAVSEGVLPGAGTSFVKASLRLGDIPTNNFDQKLGVEIVRKAITRPAQTILENAGLEGNLIVGKLKELYGKEFNIGYDIAKDRFVDLNEIGVLDPLKVVRTGLVDASGVASLMGTTECAIVDAPEESKAPAGPPGMGGMGGMPGMM
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
77PhosphorylationLIDQPFGSPKITKDG
EEECCCCCCCCCCCC
24.3328889911
90PhosphorylationDGVTVARSVSLKDKF
CCEEEEEECCHHHHH
13.3021712547
92PhosphorylationVTVARSVSLKDKFEN
EEEEEECCHHHHHHH
30.8328889911
110PhosphorylationRLVQDVASKTNEVAG
HHHHHHHHHCCCCCC
39.6021712547
232PhosphorylationKFDRGYISPYFITDV
CCCCCCCCCEEEEEC
12.6925720772
241PhosphorylationYFITDVKSQKVEFEN
EEEEECCCCCEEECC
34.7725720772
259PhosphorylationLLSEKKVSAVQDILP
EEECCHHHHHHHHHH
31.4425720772
416PhosphorylationAVIKVGGSSEVEVNE
EEEEECCCCCEEECC
19.8724763107
417PhosphorylationVIKVGGSSEVEVNEK
EEEECCCCCEEECCC
49.2724763107

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 HSP60_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSP60_SCHPO !!

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 HSP60_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of HSP60_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSP60_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-92, AND MASSSPECTROMETRY.

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