YFYB_SCHPO - dbPTM
YFYB_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YFYB_SCHPO
UniProt AC Q9UT17
Protein Name Uncharacterized protein C9.11
Gene Name SPAC9.11
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 328
Subcellular Localization Cytoplasm . Nucleus .
Protein Description
Protein Sequence MDSANKNTKIFAEQLGNDFTISVDDEDMEMEYPLRSSTPTKVIDDQREILLQKASRISKLDEALCELNNESNGSIDLSIDSFIPSYDEFLHKKLLNEDTGHESKVSDQVKQVISTPMSTCFEQWFEGEEQSSTGNNQDISYSSVNSLSPKRRGISLMSIDANKLSPKKTSPNSGYITSPLRHPILLSETEPGTPTKNDSPAYIGLPSQPNSITTLNNTNQKFQVPDNDKPPMSSLNELSASYKPIVFDSSQHKTQGTDNNDSFYHDDTNCIHLSRLEKIRELLTFVQLELKYYVEPLKKELQETKTLLAQKEEEISNLKDKLQNAGLS
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
36PhosphorylationEMEYPLRSSTPTKVI
CEEEECCCCCCCEEC
46.3729996109
37PhosphorylationMEYPLRSSTPTKVID
EEEECCCCCCCEECC
31.7829996109
38PhosphorylationEYPLRSSTPTKVIDD
EEECCCCCCCEECCH
35.9029996109
40PhosphorylationPLRSSTPTKVIDDQR
ECCCCCCCEECCHHH
37.7225720772
99PhosphorylationKKLLNEDTGHESKVS
HHHCCCCCCCHHHCH
33.9724763107
103PhosphorylationNEDTGHESKVSDQVK
CCCCCCHHHCHHHHH
32.4624763107
106PhosphorylationTGHESKVSDQVKQVI
CCCHHHCHHHHHHHH
26.5121712547
155PhosphorylationSPKRRGISLMSIDAN
CCCCCCEEEEEEECC
22.3524763107
158PhosphorylationRRGISLMSIDANKLS
CCCEEEEEEECCCCC
23.7024763107
165PhosphorylationSIDANKLSPKKTSPN
EEECCCCCCCCCCCC
35.9624763107
169PhosphorylationNKLSPKKTSPNSGYI
CCCCCCCCCCCCCCC
56.3924763107
170PhosphorylationKLSPKKTSPNSGYIT
CCCCCCCCCCCCCCC
30.8528889911
173PhosphorylationPKKTSPNSGYITSPL
CCCCCCCCCCCCCCC
36.0421712547
175PhosphorylationKTSPNSGYITSPLRH
CCCCCCCCCCCCCCC
10.8021712547
177PhosphorylationSPNSGYITSPLRHPI
CCCCCCCCCCCCCCE
18.7927738172
187PhosphorylationLRHPILLSETEPGTP
CCCCEEECCCCCCCC
38.7421712547
189PhosphorylationHPILLSETEPGTPTK
CCEEECCCCCCCCCC
44.0721712547
193PhosphorylationLSETEPGTPTKNDSP
ECCCCCCCCCCCCCC
38.2021712547
195PhosphorylationETEPGTPTKNDSPAY
CCCCCCCCCCCCCCC
42.1727738172
207PhosphorylationPAYIGLPSQPNSITT
CCCCCCCCCCCCEEE
64.4124763107
211PhosphorylationGLPSQPNSITTLNNT
CCCCCCCCEEECCCC
28.1724763107
254PhosphorylationFDSSQHKTQGTDNND
EECCCCCCCCCCCCC
30.0629996109
257PhosphorylationSQHKTQGTDNNDSFY
CCCCCCCCCCCCCCC
26.2429996109
262PhosphorylationQGTDNNDSFYHDDTN
CCCCCCCCCCCCCCC
29.8129996109
264PhosphorylationTDNNDSFYHDDTNCI
CCCCCCCCCCCCCEE
14.3229996109

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 YFYB_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YFYB_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 YFYB_SCHPO !!

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

Oops, there are no PPI records of YFYB_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YFYB_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-170, AND MASSSPECTROMETRY.

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