PGM3_YEAST - dbPTM
PGM3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGM3_YEAST
UniProt AC Q03262
Protein Name Phosphoribomutase {ECO:0000303|PubMed:23103740}
Gene Name PRM15 {ECO:0000303|PubMed:23670538}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 622
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Major phosphoribomutase that converts ribose 1-phosphate to ribose 5-phosphate. Involved in ribose salvage via the pentose phosphate pathway..
Protein Sequence MLQGILETVPSDLKDPISLWFKQDRNPKTIEEVTALCKKSDWNELHKRFDSRIQFGTAGLRSQMQAGFSRMNTLVVIQASQGLATYVRQQFPDNLVAVVGHDHRFHSKEFARATAAAFLLKGFKVHYLNPDHEFVHTPLVPFAVDKLKASVGVMITASHNPKMDNGYKVYYSNGCQIIPPHDHAISDSIDANLEPWANVWDFDDVLNKALKQGKLMYSREEMLKLYLEEVSKNLVEINPLKLEVKAKPWFVYTPMHGVGFDIFSTIVKKTLCLVEGKDYLCVPEQQNPDPSFPTVGFPNPEEKGALDIGINLAEKHDIDLLVANDPDADRFSVAVKDMQSGEWRQLTGNEIGFLFAFYEYQKYKSMDKEFQHVHPLAMLNSTVSSQMIKKMAEIEGFHYEDTLTGFKWIGNRAILLEKKGYYVPFGFEEAIGYMFPAMEHDKDGISASIVFLQAYCKWKIDHNLDPLNVLENGFKKYGVFKEYNGYYVVPNPTVTKDIFDYIRNVYTPEGASYPSSIGEEIEVLYYRDLTTGYQSDTINHKPTLPVDPTSQMITVSARPSNGSENEHIRFTIRGSGTEPKLKVYIEACANEEQRASFLAKLTWNVLRREWFRPDEMNIVTKF
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
8PhosphorylationMLQGILETVPSDLKD
CCCCHHHCCCCCCCC		33.9819795423
11PhosphorylationGILETVPSDLKDPIS
CHHHCCCCCCCCHHH		51.7619795423
121AcetylationTAAAFLLKGFKVHYL
HHHHHHHHCCEEEEE		65.5322865919
150PhosphorylationAVDKLKASVGVMITA
HHHHHHEEEEEEEEE		20.1622890988
156PhosphorylationASVGVMITASHNPKM
EEEEEEEEECCCCCC		12.1922369663
158PhosphorylationVGVMITASHNPKMDN
EEEEEEECCCCCCCC		18.3622369663
332PhosphorylationDPDADRFSVAVKDMQ
CCCCCCEEEEEEECC		15.2928889911
340PhosphorylationVAVKDMQSGEWRQLT
EEEEECCCCCCEECC		31.8528889911
399PhosphorylationAEIEGFHYEDTLTGF
HHCCCCCEECCCCCC		17.1528889911
402PhosphorylationEGFHYEDTLTGFKWI
CCCCEECCCCCCEEE		17.8028889911
404PhosphorylationFHYEDTLTGFKWIGN
CCEECCCCCCEEECC		42.5428889911
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 PGM3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGM3_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 PGM3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEC7_YEASTSEC7genetic
27708008
APC11_YEASTAPC11genetic
27708008
CP51_YEASTERG11genetic
27708008
PRS7_YEASTRPT1genetic
27708008
TAD3_YEASTTAD3genetic
27708008
SIF2_YEASTSIF2genetic
27708008
AIM4_YEASTAIM4genetic
27708008
ELO2_YEASTELO2genetic
27708008
THRC_YEASTTHR4genetic
27708008
SAC3_YEASTSAC3genetic
27708008
UME6_YEASTUME6genetic
27708008
H2A1_YEASTHTA1genetic
27708008
YD286_YEASTYDR286Cgenetic
27708008
IES5_YEASTIES5genetic
27708008
IES1_YEASTIES1genetic
27708008
MED5_YEASTNUT1genetic
27708008
YJ24_YEASTKCH1genetic
27708008
ERG3_YEASTERG3genetic
27708008
PEX13_YEASTPEX13genetic
27708008
EIF3J_YEASTHCR1genetic
27708008
LIPB_YEASTLIP2genetic
27708008
RL26A_YEASTRPL26Agenetic
27708008
GTR1_YEASTGTR1genetic
27708008
HDA1_YEASTHDA1genetic
27708008
OCA1_YEASTOCA1genetic
27708008
YO105_YEASTYOR105Wgenetic
27708008
NAA30_YEASTMAK3genetic
27708008
MED1_YEASTMED1genetic
27708008
CPSF5_HUMANNUDT21physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PGM3_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 THR-156 AND SER-158, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, AND MASSSPECTROMETRY.

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