AROG_YEAST - dbPTM
AROG_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AROG_YEAST
UniProt AC P32449
Protein Name Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited
Gene Name ARO4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 370
Subcellular Localization
Protein Description Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP)..
Protein Sequence MSESPMFAANGMPKVNQGAEEDVRILGYDPLASPALLQVQIPATPTSLETAKRGRREAIDIITGKDDRVLVIVGPCSIHDLEAAQEYALRLKKLSDELKGDLSIIMRAYLEKPRTTVGWKGLINDPDVNNTFNINKGLQSARQLFVNLTNIGLPIGSEMLDTISPQYLADLVSFGAIGARTTESQLHRELASGLSFPVGFKNGTDGTLNVAVDACQAAAHSHHFMGVTKHGVAAITTTKGNEHCFVILRGGKKGTNYDAKSVAEAKAQLPAGSNGLMIDYSHGNSNKDFRNQPKVNDVVCEQIANGENAITGVMIESNINEGNQGIPAEGKAGLKYGVSITDACIGWETTEDVLRKLAAAVRQRREVNKK
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
2Phosphorylation------MSESPMFAA
------CCCCCCCCC		46.9422369663
2Acetylation------MSESPMFAA
------CCCCCCCCC		46.9422814378
4Phosphorylation----MSESPMFAANG
----CCCCCCCCCCC		17.8522369663
28PhosphorylationEDVRILGYDPLASPA
HCEEECCCCCCCCCE		15.7922369663
33PhosphorylationLGYDPLASPALLQVQ
CCCCCCCCCEEEEEE		20.5622369663
44PhosphorylationLQVQIPATPTSLETA
EEEECCCCCCCHHHH		23.0322369663
46PhosphorylationVQIPATPTSLETAKR
EECCCCCCCHHHHHC		41.4022369663
47PhosphorylationQIPATPTSLETAKRG
ECCCCCCCHHHHHCC		25.9722369663
50PhosphorylationATPTSLETAKRGRRE
CCCCCHHHHHCCCHH		42.6522369663
52UbiquitinationPTSLETAKRGRREAI
CCCHHHHHCCCHHHH		63.9117644757
65AcetylationAIDIITGKDDRVLVI
HHEEEECCCCEEEEE		48.0524489116
652-HydroxyisobutyrylationAIDIITGKDDRVLVI
HHEEEECCCCEEEEE		48.05-
65SuccinylationAIDIITGKDDRVLVI
HHEEEECCCCEEEEE		48.0523954790
95PhosphorylationALRLKKLSDELKGDL
HHHHHHHCHHHCCCH		37.6130377154
120UbiquitinationPRTTVGWKGLINDPD
CCCCCCCCCCCCCCC		37.6023749301
136UbiquitinationNNTFNINKGLQSARQ
CCCCCCCHHHHHHHH		58.1423749301
136AcetylationNNTFNINKGLQSARQ
CCCCCCCHHHHHHHH		58.1424489116
184PhosphorylationIGARTTESQLHRELA
CCCCCCHHHHHHHHH		35.6323749301
195PhosphorylationRELASGLSFPVGFKN
HHHHHCCCCCEEEEC		30.9129734811
201AcetylationLSFPVGFKNGTDGTL
CCCCEEEECCCCCCE		48.8424489116
260AcetylationKGTNYDAKSVAEAKA
CCCCCCHHHHHHHHH		42.4325381059
287AcetylationYSHGNSNKDFRNQPK
CCCCCCCCCCCCCCC		59.0524489116
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 AROG_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AROG_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 AROG_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TCTP_YEASTTMA19physical
16554755
SMT3_YEASTSMT3physical
18719252
ASK10_YEASTASK10genetic
20093466
MSS18_YEASTMSS18genetic
20093466
ELO2_YEASTELO2genetic
21623372
FABG_YEASTOAR1genetic
21623372
THRC_YEASTTHR4genetic
21623372
DCOR_YEASTSPE1genetic
21623372
NDK_YEASTYNK1genetic
21623372
ATPO_YEASTATP5genetic
21623372
IMG2_YEASTIMG2genetic
27708008
MCH1_YEASTMCH1genetic
27708008
RXT3_YEASTRXT3genetic
27708008
IMP2_YEASTIMP2genetic
27708008
SIN3_YEASTSIN3genetic
27708008
CBS_HUMANCBSphysical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AROG_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-2; SER-4; THR-44 ANDSER-47, AND MASS SPECTROMETRY.

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