HSP90_SCHPO - dbPTM
HSP90_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSP90_SCHPO
UniProt AC P41887
Protein Name Heat shock protein 90 homolog
Gene Name swo1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 704
Subcellular Localization Cytoplasm.
Protein Description Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity). Interacts with the wee1 protein kinase; which requires swo1 for its activation..
Protein Sequence MSNTETFKFEAEISQLMSLIINTVYSNKEIFLRELISNASDALDKIRYQSLSDPHALDAEKDLFIRITPDKENKILSIRDTGIGMTKNDLINNLGVIAKSGTKQFMEAAASGADISMIGQFGVGFYSAYLVADKVQVVSKHNDDEQYIWESSAGGSFTVTLDTDGPRLLRGTEIRLFMKEDQLQYLEEKTIKDTVKKHSEFISYPIQLVVTREVEKEVPEEEETEEVKNEEDDKAPKIEEVDDESEKKEKKTKKVKETTTETEELNKTKPIWTRNPSEVTKEEYASFYKSLTNDWEDHLAVKHFSVEGQLEFRAILFVPRRAPMDLFEAKRKKNNIKLYVRRVFITDDCEELIPEWLGFIKGVVDSEDLPLNLSREMLQQNKIMKVIRKNLVRRCLDMFNEIAEDKENFKTFYDAFSKNLKLGIHEDAANRPALAKLLRYNSLNSPDDLISLEDYITKMPEHQKNIYFITGESKQAVENSPFLEIFRAKKFDVLFMVDPIDEYAVTQLKEFEGKKLVNITKDGLELEETDEEKAAREKLEKEYEEFAKQLKTILGDKVEKVVVSNKIVGSPCLLTTGQYGWSANMERIMKAQALRDTSMSAYMSSRKTFEINPKSPIIAELKKKVEENGAEDRSVKDLATILYETALLSSGFTLDDPSAYAQRINRLISLGLSIDEEEEAPIEEISTESVAAENNAESKMEEVD
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
50PhosphorylationLDKIRYQSLSDPHAL
HHHHHHHHCCCCCCC		22.3925720772
68PhosphorylationKDLFIRITPDKENKI
CCEEEEECCCCCCCE		18.6524763107
199PhosphorylationKDTVKKHSEFISYPI
HHHHHHHHHHHCCCE		42.9825720772
224PhosphorylationEVPEEEETEEVKNEE
CCCCHHHCHHHCCCC		40.5021712547
245PhosphorylationIEEVDDESEKKEKKT
HHHCCCHHHHHHHHC		62.8128889911
268PhosphorylationETEELNKTKPIWTRN
CHHHHHCCCCCCCCC		40.7621712547
273PhosphorylationNKTKPIWTRNPSEVT
HCCCCCCCCCHHHCC		22.6821712547
277PhosphorylationPIWTRNPSEVTKEEY
CCCCCCHHHCCHHHH		48.5328889911
280PhosphorylationTRNPSEVTKEEYASF
CCCHHHCCHHHHHHH		28.7821712547
286PhosphorylationVTKEEYASFYKSLTN
CCHHHHHHHHHHHCC		28.3628889911
290PhosphorylationEYASFYKSLTNDWED
HHHHHHHHHCCCHHH		29.1028889911
292PhosphorylationASFYKSLTNDWEDHL
HHHHHHHCCCHHHCE		37.9228889911
366PhosphorylationFIKGVVDSEDLPLNL
HHHCCCCCCCCCCCC		22.7728889911
374PhosphorylationEDLPLNLSREMLQQN
CCCCCCCCHHHHHHC		25.7328889911
417PhosphorylationKTFYDAFSKNLKLGI
HHHHHHHHHHCCCCC		23.5025720772
440PhosphorylationALAKLLRYNSLNSPD
HHHHHHHHCCCCCHH		14.7425720772
442PhosphorylationAKLLRYNSLNSPDDL
HHHHHHCCCCCHHHC		21.7225720772
445PhosphorylationLRYNSLNSPDDLISL
HHHCCCCCHHHCCCH		34.6929996109
451PhosphorylationNSPDDLISLEDYITK
CCHHHCCCHHHHHHH		32.7624763107
473PhosphorylationIYFITGESKQAVENS
EEEEECCCHHHHHCC		31.2625720772
480PhosphorylationSKQAVENSPFLEIFR
CHHHHHCCCHHHHHH		11.9725720772
597PhosphorylationKAQALRDTSMSAYMS
HHHHHHHCCHHHHHH		21.6429996109
598PhosphorylationAQALRDTSMSAYMSS
HHHHHHCCHHHHHHC		18.2829996109
600PhosphorylationALRDTSMSAYMSSRK
HHHHCCHHHHHHCCC		18.9325720772
602PhosphorylationRDTSMSAYMSSRKTF
HHCCHHHHHHCCCCE		7.1025720772
608PhosphorylationAYMSSRKTFEINPKS
HHHHCCCCEECCCCC		25.9525720772
615PhosphorylationTFEINPKSPIIAELK
CEECCCCCHHHHHHH		23.6928889911
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 HSP90_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSP90_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 HSP90_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP2C1_SCHPOptc1genetic
8196617
MYO2_SCHPOmyo2genetic
15755919
RNG3_SCHPOrng3genetic
15755919
MYO2_SCHPOmyo2physical
15755919
PLO1_SCHPOplo1genetic
22543982
CDK1_SCHPOcdc2genetic
22543982
SID2_SCHPOsid2genetic
22543982
CDC7_SCHPOcdc7genetic
22543982
CDK1_SCHPOcdc2physical
22543982
PLO1_SCHPOplo1physical
22543982
PYP1_SCHPOpyp1genetic
8832414
HSP90_SCHPOhsp90physical
23664927
STI1_SCHPOsti1physical
23664927
YNY8_SCHPOaha1physical
23664927
CYAA_SCHPOcyr1genetic
1849107
YNY8_SCHPOaha1physical
26771498
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSP90_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-245; SER-277 ANDSER-286, AND MASS SPECTROMETRY.

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