KPR1_YEAST - dbPTM
KPR1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KPR1_YEAST
UniProt AC P32895
Protein Name Ribose-phosphate pyrophosphokinase 1
Gene Name PRS1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 427
Subcellular Localization Cytoplasm .
Protein Description 5-phosphoribose 1-diphosphate synthase involved in nucleotide, histidine, and tryptophan biosynthesis. Active in heteromultimeric complexes with other 5-phosphoribose 1-diphosphate synthases (PRS2, PRS3, PRS4 and PRS5)..
Protein Sequence MRKCKIFVGNSHPELGNMVCQRLGIEPAPCTLKKFANGETSVQIGVSVRDEDVYVIQSGSPSINDDIMELLILVSACRGGSARKITAVIPQFPYSKQCKMKRHRGAITARMLANLLVMAGADHVVSMDLHASQMQGFFTKPVDNLYGGPSLAKWIRENVEDYEDAVVVSKNPGGTKRVTALADSLKINFAMIHTDRRRSKDLYSQNKDLQQLKLRKQSMLRKNRPIIRQGDHPNEEENIILSNGIQTARIRNGHVIGDDEADDDEDAILESDSELHSIDGLDSHGLGGTYDAVDSEDEEEIPVLYREQLITLVGNVRGRSAIILDDMIDRPGSFISAAEHLVQNCGAKKVYVVATHGIFTGDCLEELEKSDAIDTIVVTNTYPISGERIAGSKKLVTIDVSPIFAECIRRDHYGESISVLFDSLAAL
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
5Ubiquitination---MRKCKIFVGNSH
---CCCCEEEECCCC		42.0623749301
33UbiquitinationEPAPCTLKKFANGET
CCCCCEEEECCCCCC		27.9122817900
34UbiquitinationPAPCTLKKFANGETS
CCCCEEEECCCCCCE		53.4722817900
40PhosphorylationKKFANGETSVQIGVS
EECCCCCCEEEEECE		35.2828889911
47PhosphorylationTSVQIGVSVRDEDVY
CEEEEECEECCCCEE		13.2628889911
96AcetylationIPQFPYSKQCKMKRH
CCCCCCCCCCCCCCC		54.6022865919
170UbiquitinationEDAVVVSKNPGGTKR
CCCEEEECCCCCCHH		56.4023749301
179PhosphorylationPGGTKRVTALADSLK
CCCCHHHEHHHHHHE		21.7128889911
194PhosphorylationINFAMIHTDRRRSKD
EEEEEEECCCHHCHH		21.9228889911
199PhosphorylationIHTDRRRSKDLYSQN
EECCCHHCHHHHHCC		28.8021082442
200AcetylationHTDRRRSKDLYSQNK
ECCCHHCHHHHHCCC		50.3625381059
203PhosphorylationRRRSKDLYSQNKDLQ
CHHCHHHHHCCCCHH		20.5328889911
207AcetylationKDLYSQNKDLQQLKL
HHHHHCCCCHHHHHH		52.7824489116
213AcetylationNKDLQQLKLRKQSML
CCCHHHHHHHHHHHH		41.7424489116
218PhosphorylationQLKLRKQSMLRKNRP
HHHHHHHHHHHCCCC		23.8722890988
271PhosphorylationDEDAILESDSELHSI
CCCHHCCCCCCCCCC		42.8828889911
277PhosphorylationESDSELHSIDGLDSH
CCCCCCCCCCCCCCC		34.6928889911
290PhosphorylationSHGLGGTYDAVDSED
CCCCCCCEECCCCCC		12.7428889911
295PhosphorylationGTYDAVDSEDEEEIP
CCEECCCCCCHHHCC		40.1127214570
348UbiquitinationLVQNCGAKKVYVVAT
HHHHCCCCEEEEEEE		28.2317644757
349UbiquitinationVQNCGAKKVYVVATH
HHHCCCCEEEEEEEC		37.9617644757
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 KPR1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KPR1_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 KPR1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KPR2_YEASTPRS2physical
11283351
TUP1_YEASTTUP1physical
11297736
KPR3_YEASTPRS3physical
10212224
KPR2_YEASTPRS2physical
10212224
KPR3_YEASTPRS3genetic
15470112
KPR3_YEASTPRS3physical
11283351
KPR5_YEASTPRS5physical
18467557
KPR1_YEASTPRS1physical
18467557
KPR3_YEASTPRS3physical
18719252
KPR5_YEASTPRS5physical
22615397
KPR5_YEASTPRS5genetic
23368839
RLM1_YEASTRLM1physical
27744273
KPRA_HUMANPRPSAP1physical
27107014
PRPS1_HUMANPRPS1physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KPR1_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-199; SER-271; SER-277;TYR-290 AND SER-295, AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-218, ANDMASS SPECTROMETRY.

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