YAS2_SCHPO - dbPTM
YAS2_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YAS2_SCHPO
UniProt AC Q10138
Protein Name CRAL-TRIO domain-containing protein C3H8.02
Gene Name SPAC3H8.02
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 444
Subcellular Localization
Protein Description
Protein Sequence MPEGAGRPWNLTELEEEKLKTMWSYLFKLFGITLLERTESWYTVKTHLSDDSSSSSSHRLSSVSYAKSRTRLELTSSSHGSDTRSFNDKTKNVHLERVEKIASEWDPEGLRVCFWDAVNCDDPDGLLLRFLRARKWNVEAALEMFMKTVHWRSREMNVGEIVCNADHLDKDDDFVRQLRIGKCFIFGEDKHNRPVCYIRARLHKVGDVSPESVERLTVWVMETARLILKPPIETATVVFDMTDFSMSNMDYGPLKFMIKCFEAHYPECLGECIVHKAPWLFQGVWSIIKSWLDPVVVSKVKFTRNYRDLQQYINPDNILKEFGGPNPWRYTYPEPCQNEAEALKNVEARKSLRAKKDAIAKQYEEVTMDWILNNGDMAEVKQKRRKLASQLIDAYWNLDKYIRARSVYDRMGLIAPQTSHTLLLSQPTNGDVKESMVEVTSSAT
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
33PhosphorylationLFKLFGITLLERTES
HHHHHCCHHHEECCC
26.1821712547
38PhosphorylationGITLLERTESWYTVK
CCHHHEECCCEEEEE
25.6221712547
40PhosphorylationTLLERTESWYTVKTH
HHHEECCCEEEEEEE
25.4428889911
42PhosphorylationLERTESWYTVKTHLS
HEECCCEEEEEEECC
15.7821712547
43PhosphorylationERTESWYTVKTHLSD
EECCCEEEEEEECCC
14.8528889911
49PhosphorylationYTVKTHLSDDSSSSS
EEEEEECCCCCCCCC
31.5929996109
52PhosphorylationKTHLSDDSSSSSSHR
EEECCCCCCCCCCCC
36.7929996109
61PhosphorylationSSSSHRLSSVSYAKS
CCCCCCCCCCEEECC
28.7525720772
62PhosphorylationSSSHRLSSVSYAKSR
CCCCCCCCCEEECCC
21.4825720772
64PhosphorylationSHRLSSVSYAKSRTR
CCCCCCCEEECCCCE
22.7125720772
65PhosphorylationHRLSSVSYAKSRTRL
CCCCCCEEECCCCEE
18.8525720772
68PhosphorylationSSVSYAKSRTRLELT
CCCEEECCCCEEEEE
30.6121712547
70PhosphorylationVSYAKSRTRLELTSS
CEEECCCCEEEEECC
46.8525720772
75PhosphorylationSRTRLELTSSSHGSD
CCCEEEEECCCCCCC
19.7225720772
76PhosphorylationRTRLELTSSSHGSDT
CCEEEEECCCCCCCC
42.3329996109
77PhosphorylationTRLELTSSSHGSDTR
CEEEEECCCCCCCCC
22.5629996109
78PhosphorylationRLELTSSSHGSDTRS
EEEEECCCCCCCCCC
31.4729996109
81PhosphorylationLTSSSHGSDTRSFND
EECCCCCCCCCCCCH
30.3128889911
83PhosphorylationSSSHGSDTRSFNDKT
CCCCCCCCCCCCHHC
29.8829996109
85PhosphorylationSHGSDTRSFNDKTKN
CCCCCCCCCCHHCCC
30.4125720772
418PhosphorylationMGLIAPQTSHTLLLS
HCCCCCCCCCEEEEC
22.7828889911
419PhosphorylationGLIAPQTSHTLLLSQ
CCCCCCCCCEEEECC
14.8229996109
421PhosphorylationIAPQTSHTLLLSQPT
CCCCCCCEEEECCCC
20.9025720772
425PhosphorylationTSHTLLLSQPTNGDV
CCCEEEECCCCCCCC
33.8029996109
428PhosphorylationTLLLSQPTNGDVKES
EEEECCCCCCCCCHH
44.1725720772
441PhosphorylationESMVEVTSSAT----
HHHEEEECCCC----
24.1325720772

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 YAS2_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YAS2_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 YAS2_SCHPO !!

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

Oops, there are no PPI records of YAS2_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YAS2_SCHPO

loading...

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-40; THR-43; SER-81 ANDTHR-418, AND MASS SPECTROMETRY.

TOP