PGK_SCHPO - dbPTM
PGK_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGK_SCHPO
UniProt AC O60101
Protein Name Phosphoglycerate kinase
Gene Name pgk1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 414
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MSLSTKLAITDVDLKGKNVLIRVDFNVPLDGDRITNNARIVGALPTIKYALEQQPKAVILMSHLGRPNGARVAKYSLKPVAAELSKLLGKPVKFLDDCVGPEVEKACKEAKGGEVILLENLRFHIEEEGSAKVDGKKVKADASAVEAFRKSLTSLGDIFVNDAFGTAHRAHSSMVGVDLPRVSGFLMKKELDYFSKALENPARPFLAILGGAKVADKIQLIDNLLDKVNRLIICGGMAFTFLKVLNGMKIGDSLFDEAGSKNVESMMAKAKKNNVEVFLPVDFVTADKFDKDAKVGSATAEEGIPDGWMGLDCGPKSSAKFAEVITTSKTIVWNGPAGVFEFDNFAKGTKSMLDACVKTCEAGNVVIVGGGDTATVAKKYGKEDALSHVSTGGGASLELLEGKALPGVVALSSK
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
35PhosphorylationPLDGDRITNNARIVG
CCCCCCCCCCCEEEE		24.2628889911
75PhosphorylationNGARVAKYSLKPVAA
CCCCCCCCCCHHHHH		14.9728889911
76PhosphorylationGARVAKYSLKPVAAE
CCCCCCCCCHHHHHH		29.2528889911
143PhosphorylationKKVKADASAVEAFRK
EEEECCHHHHHHHHH		33.1328889911
151PhosphorylationAVEAFRKSLTSLGDI
HHHHHHHHHHHHHHH		32.4029996109
153PhosphorylationEAFRKSLTSLGDIFV
HHHHHHHHHHHHHHH		29.0629996109
154PhosphorylationAFRKSLTSLGDIFVN
HHHHHHHHHHHHHHC		35.3329996109
172PhosphorylationGTAHRAHSSMVGVDL
CCCCHHHHHCCCCCC		21.1028889911
173PhosphorylationTAHRAHSSMVGVDLP
CCCHHHHHCCCCCCC		13.9728889911
183PhosphorylationGVDLPRVSGFLMKKE
CCCCCCCCCCCCHHH		25.7128889911
195PhosphorylationKKELDYFSKALENPA
HHHHHHHHHHHHCCC		15.7028889911
253PhosphorylationNGMKIGDSLFDEAGS
CCCCCCCHHCHHHCC		26.2328889911
260PhosphorylationSLFDEAGSKNVESMM
HHCHHHCCCCHHHHH		28.2728889911
297PhosphorylationDKDAKVGSATAEEGI
CCCCCCCCCCCCCCC		25.9827738172
299PhosphorylationDAKVGSATAEEGIPD
CCCCCCCCCCCCCCC		35.9828889911
326PhosphorylationAKFAEVITTSKTIVW
HHHHEEEECCCEEEE		30.1425720772
327PhosphorylationKFAEVITTSKTIVWN
HHHEEEECCCEEEEC		19.6625720772
328PhosphorylationFAEVITTSKTIVWNG
HHEEEECCCEEEECC		21.1028889911
351PhosphorylationNFAKGTKSMLDACVK
CCCCCCHHHHHHHHH		25.1528889911
373PhosphorylationVIVGGGDTATVAKKY
EEECCCCHHHHHHHH		27.7428889911
375PhosphorylationVGGGDTATVAKKYGK
ECCCCHHHHHHHHCC		24.0825720772
387PhosphorylationYGKEDALSHVSTGGG
HCCCCHHHCCCCCCC		24.4628889911
390PhosphorylationEDALSHVSTGGGASL
CCHHHCCCCCCCHHH		18.8628889911
391PhosphorylationDALSHVSTGGGASLE
CHHHCCCCCCCHHHH		38.4621712547
396PhosphorylationVSTGGGASLELLEGK
CCCCCCHHHHHHCCC		26.1721712547
412PhosphorylationLPGVVALSSK-----
CCCEEEECCC-----		26.7528889911
413PhosphorylationPGVVALSSK------
CCEEEECCC------		43.1428889911
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 PGK_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGK_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 PGK_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PGK_SCHPO !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PGK_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 TYR-75; SER-76; SER-143;SER-172; SER-173; SER-183; SER-253; SER-260; THR-299; SER-328;SER-351; THR-373; SER-387; SER-390; SER-412 AND SER-413, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory