PUR2_YEAST - dbPTM
PUR2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PUR2_YEAST
UniProt AC P07244
Protein Name Bifunctional purine biosynthetic protein ADE5,7
Gene Name ADE5,7
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 802
Subcellular Localization
Protein Description
Protein Sequence MLNILVLGNGAREHVLVTKLAQSPTVGKIYVAPGNGGTATMDPSRVINWDITPDVANFARLQSMAVEHKINLVVPGPELPLVNGITSVFHSVGIPVFGPSVKAAQLEASKAFSKRFMSKHNIPTASYDVFTNPEEAISFLQAHTDKAFVIKADGIAAGKGVIIPSSIDESVQAIKDIMVTKQFGEEAGKQVVIEQFLEGDEISLLTIVDGYSHFNLPVAQDHKRIFDGDKGLNTGGMGAYAPAPVATPSLLKTIDSQIVKPTIDGMRRDGMPFVGVLFTGMILVKDSKTNQLVPEVLEYNVRFGDPETQAVLSLLDDQTDLAQVFLAAAEHRLDSVNIGIDDTRSAVTVVVAAGGYPESYAKGDKITLDTDKLPPHTQIFQAGTKYDSATDSLLTNGGRVLSVTSTAQDLRTAVDTVYEAVKCVHFQNSYYRKDIAYRAFQNSESSKVAITYADSGVSVDNGNNLVQTIKEMVRSTRRPGADSDIGGFGGLFDLAQAGFRQNEDTLLVGATDGVGTKLIIAQETGIHNTVGIDLVAMNVNDLVVQGAEPLFFLDYFATGALDIQVASDFVSGVANGCIQSGCALVGGETSEMPGMYPPGHYDTNGTAVGAVLRQDILPKINEMAAGDVLLGLASSGVHSNGFSLVRKIIQHVALPWDAPCPWDESKTLGEGILEPTKIYVKQLLPSIRQRLLLGLAHITGGGLVENIPRAIPDHLQARVDMSTWEVPRVFKWFGQAGNVPHDDILRTFNMGVGMVLIVKRENVKAVCDSLTEEGEIIWELGSLQERPKDAPGCVIENGTKLY
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
19UbiquitinationREHVLVTKLAQSPTV
CEEEEEEEECCCCCC		34.0523749301
23PhosphorylationLVTKLAQSPTVGKIY
EEEEECCCCCCCEEE		19.5522369663
25PhosphorylationTKLAQSPTVGKIYVA
EEECCCCCCCEEEEE		47.3322369663
28UbiquitinationAQSPTVGKIYVAPGN
CCCCCCCEEEEECCC		26.9123749301
119UbiquitinationFSKRFMSKHNIPTAS
HHHHHHHHCCCCCCC		28.9617644757
146UbiquitinationFLQAHTDKAFVIKAD
HHHHCCCCEEEEECC		44.9017644757
159UbiquitinationADGIAAGKGVIIPSS
CCCEECCCCEECCCC		45.3217644757
165PhosphorylationGKGVIIPSSIDESVQ
CCCEECCCCHHHHHH		29.5328889911
175UbiquitinationDESVQAIKDIMVTKQ
HHHHHHHHHHHHHHH		44.1917644757
230UbiquitinationKRIFDGDKGLNTGGM
CCCCCCCCCCCCCCC		71.4817644757
230AcetylationKRIFDGDKGLNTGGM
CCCCCCCCCCCCCCC		71.4824489116
247PhosphorylationYAPAPVATPSLLKTI
CCCCCCCCHHHHHHC		17.4025752575
249PhosphorylationPAPVATPSLLKTIDS
CCCCCCHHHHHHCCC		41.8128889911
252UbiquitinationVATPSLLKTIDSQIV
CCCHHHHHHCCCCCC		49.0417644757
253PhosphorylationATPSLLKTIDSQIVK
CCHHHHHHCCCCCCC		29.9522369663
256PhosphorylationSLLKTIDSQIVKPTI
HHHHHCCCCCCCCCC		20.2522369663
260AcetylationTIDSQIVKPTIDGMR
HCCCCCCCCCCCCCC		37.7624489116
262PhosphorylationDSQIVKPTIDGMRRD
CCCCCCCCCCCCCCC		26.4422369663
285UbiquitinationFTGMILVKDSKTNQL
EEEEEEEECCCCCCC		53.4922817900
288UbiquitinationMILVKDSKTNQLVPE
EEEEECCCCCCCCHH		62.7222817900
367PhosphorylationYAKGDKITLDTDKLP
HCCCCEEEECCCCCC		25.0727017623
370PhosphorylationGDKITLDTDKLPPHT
CCEEEECCCCCCCCC		37.8429734811
404PhosphorylationGGRVLSVTSTAQDLR
CCEEEEEECCHHHHH		19.5827017623
406PhosphorylationRVLSVTSTAQDLRTA
EEEEEECCHHHHHHH		20.9728152593
422UbiquitinationDTVYEAVKCVHFQNS
HHHHHHHHHHHCCCC		37.2717644757
445PhosphorylationRAFQNSESSKVAITY
HHHCCCCCCCEEEEE		34.9728889911
447UbiquitinationFQNSESSKVAITYAD
HCCCCCCCEEEEECC		44.9917644757
451PhosphorylationESSKVAITYADSGVS
CCCCEEEEECCCCCE		11.7022369663
452PhosphorylationSSKVAITYADSGVSV
CCCEEEEECCCCCEE		11.4222369663
455PhosphorylationVAITYADSGVSVDNG
EEEEECCCCCEECCC		32.6822369663
458PhosphorylationTYADSGVSVDNGNNL
EECCCCCEECCCCCH		27.5522369663
468PhosphorylationNGNNLVQTIKEMVRS
CCCCHHHHHHHHHHH		26.9122369663
470UbiquitinationNNLVQTIKEMVRSTR
CCHHHHHHHHHHHCC		43.0522817900
643PhosphorylationGVHSNGFSLVRKIIQ
CCCCCCHHHHHHHHH		27.6121440633
647UbiquitinationNGFSLVRKIIQHVAL
CCHHHHHHHHHHHCC		36.3617644757
666UbiquitinationPCPWDESKTLGEGIL
CCCCCCCCCCCCCCC		45.8017644757
677AcetylationEGILEPTKIYVKQLL
CCCCCCCHHHHHHHH		42.6324489116
677UbiquitinationEGILEPTKIYVKQLL
CCCCCCCHHHHHHHH		42.6322817900
681AcetylationEPTKIYVKQLLPSIR
CCCHHHHHHHHHHHH		20.4624489116
681UbiquitinationEPTKIYVKQLLPSIR
CCCHHHHHHHHHHHH		20.4624961812
731AcetylationWEVPRVFKWFGQAGN
CHHHHHHHHHCCCCC		38.4624489116
731UbiquitinationWEVPRVFKWFGQAGN
CHHHHHHHHHCCCCC		38.4622817900
800UbiquitinationCVIENGTKLY-----
CEEECCCCCC-----		47.3823749301
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 PUR2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PUR2_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 PUR2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GYS2_YEASTGSY2physical
16554755
RS3_YEASTRPS3physical
16429126
RS5_YEASTRPS5physical
16429126
FCY2_YEASTFCY2genetic
21623372
HPRT_YEASTHPT1genetic
21623372
THDH_YEASTILV1genetic
21623372
TPS1_YEASTTPS1genetic
21623372
FOLE_YEASTMET7genetic
21623372
SWC4_YEASTSWC4genetic
27708008
CDC37_YEASTCDC37genetic
27708008
RPB7_YEASTRPB7genetic
27708008
CDC4_YEASTCDC4genetic
27708008
MED6_YEASTMED6genetic
27708008
SPC97_YEASTSPC97genetic
27708008
DPB11_YEASTDPB11genetic
27708008
CDC11_YEASTCDC11genetic
27708008
RNA1_YEASTRNA1genetic
27708008
NOP8_YEASTNOP8genetic
27708008
MED4_YEASTMED4genetic
27708008
DIM1_YEASTDIM1genetic
27708008
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PUR2_YEAST

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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-165; THR-247; SER-249;THR-406; SER-455 AND SER-458, AND MASS SPECTROMETRY.

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