YHP6_SCHPO - dbPTM
YHP6_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YHP6_SCHPO
UniProt AC Q9USP7
Protein Name Uncharacterized protein C902.06
Gene Name SPBC902.06
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 397
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MSEHNYQSDREVAEDPFLNYEASANQLSSNSRESTPRGSPWRAGMRSASLMTEPLEDSMYSDNNYLDNGVSFTKDENPLYSPSWPSLADANVNSMKSNNAIQEHKAAKFVSEKSLEKVSTADNNLVLQELENLRERLNQVELQLSERPSSYLGYHNNLSPYRSPNSYPSLLPSTHSPHSPAPLSTMQTALMRLRTYHPSPIILKPVEQAVNHAITLVNTSPSSVVDALCRSLAELCLGLVQEAIDASILSQQESSNSLDLVRHTPPLNYTSSVDSSPQRMASDSYGRPSLHLNDPFPSVDLQSNELSHHNVRTTLFSDDSRFHSKIHTHSTPPSQMYSAASHFRYRSDPSTRHVSNSTNKSSLHPSPTSLRVAHPIIPQRASPASQSFPSLQDTPSP
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
2Phosphorylation------MSEHNYQSD
------CCCCCCCCC
47.7929996109
29PhosphorylationASANQLSSNSRESTP
HHHHHHCCCCCCCCC
47.6329996109
31PhosphorylationANQLSSNSRESTPRG
HHHHCCCCCCCCCCC
39.1029996109
34PhosphorylationLSSNSRESTPRGSPW
HCCCCCCCCCCCCCC
42.4725720772
35PhosphorylationSSNSRESTPRGSPWR
CCCCCCCCCCCCCCH
16.5625720772
81PhosphorylationKDENPLYSPSWPSLA
CCCCCCCCCCCCHHH
21.8221712547
83PhosphorylationENPLYSPSWPSLADA
CCCCCCCCCCHHHHH
45.7529996109
97PhosphorylationANVNSMKSNNAIQEH
HCCHHHHCCCHHHHH
27.0321712547
159PhosphorylationLGYHNNLSPYRSPNS
CCCCCCCCCCCCCCC
23.2429996109
264PhosphorylationSLDLVRHTPPLNYTS
CCCCHHCCCCCCCCC
18.9428889911
270PhosphorylationHTPPLNYTSSVDSSP
CCCCCCCCCCCCCCC
17.2929996109
271PhosphorylationTPPLNYTSSVDSSPQ
CCCCCCCCCCCCCCC
20.2929996109
272PhosphorylationPPLNYTSSVDSSPQR
CCCCCCCCCCCCCCH
23.3425720772
275PhosphorylationNYTSSVDSSPQRMAS
CCCCCCCCCCCHHCC
41.5928889911
276PhosphorylationYTSSVDSSPQRMASD
CCCCCCCCCCHHCCC
22.1629996109
289PhosphorylationSDSYGRPSLHLNDPF
CCCCCCCCCCCCCCC
27.3629996109
328PhosphorylationRFHSKIHTHSTPPSQ
HHCHHCCCCCCCHHH
22.4629996109
330PhosphorylationHSKIHTHSTPPSQMY
CHHCCCCCCCHHHHH
43.7129996109
334PhosphorylationHTHSTPPSQMYSAAS
CCCCCCHHHHHCHHH
28.8729996109
355PhosphorylationDPSTRHVSNSTNKSS
CCCCCCCCCCCCCCC
20.9525720772
361PhosphorylationVSNSTNKSSLHPSPT
CCCCCCCCCCCCCCC
39.9525720772
362PhosphorylationSNSTNKSSLHPSPTS
CCCCCCCCCCCCCCC
32.1025720772
366PhosphorylationNKSSLHPSPTSLRVA
CCCCCCCCCCCCCCC
30.0228889911
368PhosphorylationSSLHPSPTSLRVAHP
CCCCCCCCCCCCCCC
44.7425720772
369PhosphorylationSLHPSPTSLRVAHPI
CCCCCCCCCCCCCCC
19.9829996109
382PhosphorylationPIIPQRASPASQSFP
CCCCCCCCCCHHCCC
24.1625720772
394PhosphorylationSFPSLQDTPSP----
CCCCCCCCCCC----
16.8325720772
396PhosphorylationPSLQDTPSP------
CCCCCCCCC------
45.3828889911

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 YHP6_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YHP6_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 YHP6_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ALP4_SCHPOalp4physical
15837798
MBO1_SCHPOmto1physical
15659644
MBO1_SCHPOmto1physical
15800064
YHP6_SCHPOmto2physical
24704079
MBO1_SCHPOmto1physical
24704079

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YHP6_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-366 AND SER-396, ANDMASS SPECTROMETRY.

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