AROF_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AROF_YEAST
• UniProt AC: P14843
• Protein Name: Phospho-2-dehydro-3-deoxyheptonate aldolase, phenylalanine-inhibited
• Gene Name: ARO3
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 370
• 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: MFIKNDHAGDRKRLEDWRIKGYDPLTPPDLLQHEFPISAKGEENIIKARDSVCDILNGKDDRLVIVIGPCSLHDPKAAYDYADRLAKISEKLSKDLLIIMRAYLEKPRTTVGWKGLINDPDMNNSFQINKGLRISREMFIKLVEKLPIAGEMLDTISPQFLSDCFSLGAIGARTTESQLHRELASGLSFPIGFKNGTDGGLQVAIDAMRAAAHEHYFLSVTKPGVTAIVGTEGNKDTFLILRGGKNGTNFDKESVQNTKKQLEKAGLTDDSQKRIMIDCSHGNSNKDFKNQPKVAKCIYDQLTEGENSLCGVMIESNINEGRQDIPKEGGREGLKYGCSVTDACIGWESTEQVLELLAEGVRNRRKALKK

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
22	Phosphorylation	EDWRIKGYDPLTPPD HHCCCCCCCCCCCHH	14.91	22369663
26	Phosphorylation	IKGYDPLTPPDLLQH CCCCCCCCCHHHHCC	37.86	22369663
51	Phosphorylation	NIIKARDSVCDILNG CHHHHHHHHHHHHCC	21.06	28889911
59	Acetylation	VCDILNGKDDRLVIV HHHHHCCCCCEEEEE	56.22	24489116
76	Acetylation	PCSLHDPKAAYDYAD CCCCCCHHHHHHHHH	52.27	24489116
87	Ubiquitination	DYADRLAKISEKLSK HHHHHHHHHHHHHCH	51.89	23749301
94	Acetylation	KISEKLSKDLLIIMR HHHHHHCHHHHHHHH	63.93	24489116
106	Acetylation	IMRAYLEKPRTTVGW HHHHHHCCCCCCCCC	36.89	24489116
114	Acetylation	PRTTVGWKGLINDPD CCCCCCCCCCCCCCC	37.60	24489116
130	Acetylation	NNSFQINKGLRISRE CCCEECCCCCCCCHH	62.03	24489116
141	Acetylation	ISREMFIKLVEKLPI CCHHHHHHHHHHCCC	34.90	24489116
174	Phosphorylation	LGAIGARTTESQLHR HCCCCCCCCHHHHHH	34.09	22369663
175	Phosphorylation	GAIGARTTESQLHRE CCCCCCCCHHHHHHH	28.25	22369663
177	Phosphorylation	IGARTTESQLHRELA CCCCCCHHHHHHHHH	35.63	23749301
185	Phosphorylation	QLHRELASGLSFPIG HHHHHHHHCCCCEEE	53.55	22369663
188	Phosphorylation	RELASGLSFPIGFKN HHHHHCCCCEEEEEC	32.28	22369663
286	Acetylation	CSHGNSNKDFKNQPK CCCCCCCCCCCCCHH	65.45	25381059
327	Acetylation	EGRQDIPKEGGREGL CCCCCCCCCCCCCCC	70.13	25381059

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of AROF_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AROF_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of AROF_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ILV5_YEAST	ILV5	physical	16429126
AROG_YEAST	ARO4	genetic	16941010
SMI1_YEAST	SMI1	genetic	20093466
SSF1_YEAST	SSF1	genetic	20093466
YJQ3_YEAST	YJL163C	genetic	20093466
PIR5_YEAST	YJL160C	genetic	20093466
AROG_YEAST	ARO4	genetic	8625423
AROG_YEAST	ARO4	genetic	2880280
THRC_YEAST	THR4	genetic	21623372
ASK10_YEAST	ASK10	genetic	27708008
PIR5_YEAST	YJL160C	genetic	27708008
MET5_YEAST	MET5	genetic	27708008
SWI6_YEAST	SWI6	genetic	27708008
MDL2_YEAST	MDL2	genetic	27708008

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-26, AND MASSSPECTROMETRY.
PubMed: 18407956

"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 THR-26, AND MASSSPECTROMETRY.
PubMed: 17563356