YNF3_SCHPO - dbPTM
YNF3_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YNF3_SCHPO
UniProt AC Q9UUF3
Protein Name Probable tyrosine-protein phosphatase C17A3.03c
Gene Name pi043, SPBC17A3.03c
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 287
Subcellular Localization Cytoplasm . Nucleus .
Protein Description
Protein Sequence MAIVFPFQLEKKLISITSDRDQISMSIPEVSSHDSCLNDCHSVNSEEQAKPVCCLELNAHKDGIKVVDTSNDASTFSNSPLVPDNFGVVYPGIIYRSACPRASNFNFLESLHIRTIISLRQEEYSEEDLHYFTKHHINYYHIAMPGSKHRKNDCISSSSNPDISDVDDLVRKTLQLLLNKENWPVLLHCSRGKHRTGIVIGCLRALMNWPVGNRLQEYISFSHPKEREVDEEYIQNFSSDPSLKSSLNDLKRYISDSSSELADVVLSSESPTVQAATVNETCRSPGS
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
156PhosphorylationHRKNDCISSSSNPDI
CCCCCCCCCCCCCCC		30.4228889911
157PhosphorylationRKNDCISSSSNPDIS
CCCCCCCCCCCCCCC		20.2021712547
158PhosphorylationKNDCISSSSNPDISD
CCCCCCCCCCCCCCC		27.6121712547
159PhosphorylationNDCISSSSNPDISDV
CCCCCCCCCCCCCCH		55.0928889911
287PhosphorylationETCRSPGS-------
HHCCCCCC-------		40.1925720772
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 YNF3_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YNF3_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 YNF3_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HENMT_SCHPOSPBC336.05cgenetic
18818364
COX19_SCHPOSPCC1672.04cgenetic
22681890
TPP1_SCHPOtpp1genetic
22681890
ALG8_SCHPOalg8genetic
22681890
YG58_SCHPOSPBC56F2.08cgenetic
22681890
PLR2_SCHPOSPCC1281.04genetic
22681890
IMA3_SCHPOSPCC550.11genetic
22681890
YKTB_SCHPOSPAPB1E7.11cgenetic
22681890
ALG9_SCHPOalg9genetic
22681890
GCN5_SCHPOgcn5genetic
22681890
ALG10_SCHPOalg10genetic
22681890
HMT2_SCHPOhmt2genetic
22681890
TVP18_SCHPOSPBC32F12.12cgenetic
22681890
MHF2_SCHPOmhf2genetic
22681890
YE98_SCHPOerp2genetic
22681890
YJD1_SCHPOSPCC594.01genetic
22681890
ATP5E_SCHPOatp15genetic
22681890
YIDH_SCHPOSPAC227.17cgenetic
22681890
EME1_SCHPOeme1genetic
22681890
GLD1_SCHPOgld1genetic
22681890
ACH1_SCHPOSPAC1952.09cgenetic
22681890
YA4C_SCHPOSPAC31A2.12genetic
22681890
YAM5_SCHPOmso1genetic
22681890
POZ1_SCHPOpoz1genetic
22681890
APS1_SCHPOaps1genetic
22681890
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YNF3_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-156 AND SER-159, ANDMASS SPECTROMETRY.

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