YCTB_SCHPO - dbPTM
YCTB_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YCTB_SCHPO
UniProt AC P78813
Protein Name ENTH domain-containing protein C794.11c
Gene Name SPCC794.11c
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 476
Subcellular Localization
Protein Description
Protein Sequence MESIQSTMKNINLYDIKAAVRKAQNVVMNYTSMEARVREATNNEPWGASTSLMMEIAQGTHNYSQLNEILPMIYRRFTEKTAEEWRQIYKALQLLEFLVKNGSERVVDDARAHQATIKMLRNFHYIDHRQKDQGLNVRTRAKELVELLNDSERIRKERKRARQNRGKFIGVGSDGDSRISTSSKSRFPSFGSSRGSYRTRVYGDGGGFTDYGNGYHDSSSMSDSRDASDNDVEEYNEDGDGGSSDAATANSTRGSRRTTTKQSDKAPEQPKQESAMIDLLGLDNEPSPAQPQTNTSAPLAFEDDGFGDFQSSAAAPASSTLNNASLFMGSQTASTAAKNDDDAFDDFQSAPSAKPASNTAAFSSISFGGFNSLNQLPTSSSAFTPQPTTFNTGYTSAFGMSSGLSNTSSQAGLGLTSQQPTAAKSSGSNGDAFGSLWSSAVNKVHQENSTRERVVSSSSEPVSKTQNFLDNDNLLL
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
173PhosphorylationGKFIGVGSDGDSRIS
CCCEECCCCCCCCCC
35.6928889911
177PhosphorylationGVGSDGDSRISTSSK
ECCCCCCCCCCCCCC
36.7225720772
180PhosphorylationSDGDSRISTSSKSRF
CCCCCCCCCCCCCCC
22.5621712547
181PhosphorylationDGDSRISTSSKSRFP
CCCCCCCCCCCCCCC
34.3521712547
182PhosphorylationGDSRISTSSKSRFPS
CCCCCCCCCCCCCCC
29.0424763107
183PhosphorylationDSRISTSSKSRFPSF
CCCCCCCCCCCCCCC
34.4424763107
185PhosphorylationRISTSSKSRFPSFGS
CCCCCCCCCCCCCCC
40.8929996109
189PhosphorylationSSKSRFPSFGSSRGS
CCCCCCCCCCCCCCE
39.2628889911
192PhosphorylationSRFPSFGSSRGSYRT
CCCCCCCCCCCEEEE
18.1728889911
193PhosphorylationRFPSFGSSRGSYRTR
CCCCCCCCCCEEEEE
40.8329996109
215PhosphorylationFTDYGNGYHDSSSMS
CCCCCCCCCCCCCCC
13.3725720772
218PhosphorylationYGNGYHDSSSMSDSR
CCCCCCCCCCCCCCC
15.8225720772
219PhosphorylationGNGYHDSSSMSDSRD
CCCCCCCCCCCCCCC
35.8025720772
220PhosphorylationNGYHDSSSMSDSRDA
CCCCCCCCCCCCCCC
26.6828889911
222PhosphorylationYHDSSSMSDSRDASD
CCCCCCCCCCCCCCC
34.0925720772
224PhosphorylationDSSSMSDSRDASDND
CCCCCCCCCCCCCCC
25.4229996109
228PhosphorylationMSDSRDASDNDVEEY
CCCCCCCCCCCHHHH
41.0328889911
235PhosphorylationSDNDVEEYNEDGDGG
CCCCHHHHCCCCCCC
15.4528889911
243PhosphorylationNEDGDGGSSDAATAN
CCCCCCCCCCCHHCC
30.4928889911
244PhosphorylationEDGDGGSSDAATANS
CCCCCCCCCCHHCCC
34.2528889911
248PhosphorylationGGSSDAATANSTRGS
CCCCCCHHCCCCCCC
28.2625720772
425PhosphorylationQQPTAAKSSGSNGDA
CCCCCCCCCCCCCCH
34.8924763107
449PhosphorylationNKVHQENSTRERVVS
HHHHHHCCCCCEECC
28.2621712547
456PhosphorylationSTRERVVSSSSEPVS
CCCCEECCCCCCCCC
22.9624763107
457PhosphorylationTRERVVSSSSEPVSK
CCCEECCCCCCCCCC
26.6925720772
458PhosphorylationRERVVSSSSEPVSKT
CCEECCCCCCCCCCC
31.0825720772
459PhosphorylationERVVSSSSEPVSKTQ
CEECCCCCCCCCCCC
48.1128889911
463PhosphorylationSSSSEPVSKTQNFLD
CCCCCCCCCCCCCCC
40.4729996109

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 YCTB_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YCTB_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 YCTB_SCHPO !!

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

Oops, there are no PPI records of YCTB_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YCTB_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-173; SER-228; TYR-235;SER-243; SER-244 AND SER-459, AND MASS SPECTROMETRY.

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