PDXH_YEAST - dbPTM
PDXH_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDXH_YEAST
UniProt AC Q06608
Protein Name Pyridoxamine 5'-phosphate oxidase homolog
Gene Name YPR172W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 200
Subcellular Localization Cytoplasm . Nucleus .
Protein Description
Protein Sequence MAWTSTLPAHLLNLIKNSKYVHVATCSKDCIPSVALMNYIYVPGEKLFGQTDNKNDYIIFVSPQDTQKFYNIKENPKVALLFHDWIIANNLSVGKESISGTPTPTSIPHEEQRQSELLNLLQELNQAELNQMSASIGGETEIVNPESEESKYYKDLILKANPDAKAFIFEKNTAVVKVRIDNARVSNNENRTMFLSKGKS
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
54AcetylationLFGQTDNKNDYIIFV
HCCCCCCCCCEEEEE		54.7424489116
97PhosphorylationNLSVGKESISGTPTP
CCCCCCCCCCCCCCC		26.0722369663
99PhosphorylationSVGKESISGTPTPTS
CCCCCCCCCCCCCCC		45.9922369663
101PhosphorylationGKESISGTPTPTSIP
CCCCCCCCCCCCCCC		19.7322369663
103PhosphorylationESISGTPTPTSIPHE
CCCCCCCCCCCCCCH		38.7522369663
105PhosphorylationISGTPTPTSIPHEEQ
CCCCCCCCCCCCHHH		41.5922369663
106PhosphorylationSGTPTPTSIPHEEQR
CCCCCCCCCCCHHHH		35.0122369663
171AcetylationAKAFIFEKNTAVVKV
CCEEEEECCCEEEEE		49.1824489116
197AcetylationNRTMFLSKGKS----
CCEEEEECCCC----		72.9325381059
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 PDXH_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDXH_YEAST !!
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 PDXH_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDXH_YEASTYPR172Wphysical
26327315
PRP6_YEASTPRP6genetic
27708008
HEK2_YEASTHEK2genetic
27708008
FLR1_YEASTFLR1genetic
27708008
TPS1_YEASTTPS1genetic
27708008
AGP2_YEASTAGP2genetic
27708008
OCA5_YEASTOCA5genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
CND2_YEASTBRN1genetic
27708008
TIM22_YEASTTIM22genetic
27708008
ERF3_YEASTSUP35genetic
27708008
CDC1_YEASTCDC1genetic
27708008
CDC4_YEASTCDC4genetic
27708008
SWC4_YEASTSWC4genetic
27708008
SEC22_YEASTSEC22genetic
27708008
TAD3_YEASTTAD3genetic
27708008
NOP2_YEASTNOP2genetic
27708008
TYSY_YEASTCDC21genetic
27708008
RPB2_YEASTRPB2genetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
ALG3_YEASTALG3genetic
27708008
POA1_YEASTPOA1genetic
27708008
ETR1_YEASTETR1genetic
27708008
PFF1_YEASTPFF1genetic
27708008
PCL2_YEASTPCL2genetic
27708008
INO2_YEASTINO2genetic
27708008
NUP42_YEASTNUP42genetic
27708008
MET32_YEASTMET32genetic
27708008
PSP1_YEASTPSP1genetic
27708008
SPS2_YEASTSPS2genetic
27708008
VFA1_YEASTVFA1genetic
27708008
ECM32_YEASTECM32genetic
27708008
UBR1_YEASTUBR1genetic
27708008
YHI2_YEASTYHR022Cgenetic
27708008
DAP2_YEASTDAP2genetic
27708008
HXT5_YEASTHXT5genetic
27708008
PEX28_YEASTPEX28genetic
27708008
YIF4_YEASTYIL054Wgenetic
27708008
RL16A_YEASTRPL16Agenetic
27708008
CBPS_YEASTCPS1genetic
27708008
IME1_YEASTIME1genetic
27708008
YJ94_YEASTYJR124Cgenetic
27708008
HCS1_YEASTHCS1genetic
27708008
RGT1_YEASTRGT1genetic
27708008
YRA2_YEASTYRA2genetic
27708008
YKZ5_YEASTYKR015Cgenetic
27708008
PTR2_YEASTPTR2genetic
27708008
YM54_YEASTYMR196Wgenetic
27708008
RM44_YEASTMRPL44genetic
27708008
YM16A_YEASTYMR316C-Agenetic
27708008
MAS5_YEASTYDJ1genetic
27708008
SIN3_YEASTSIN3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PDXH_YEAST

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; THR-101 AND THR-103,AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND THR-101, AND MASSSPECTROMETRY.

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