ARO8_YEAST - dbPTM
ARO8_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARO8_YEAST
UniProt AC P53090
Protein Name Aromatic/aminoadipate aminotransferase 1
Gene Name ARO8
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 500
Subcellular Localization Cytoplasm .
Protein Description General aromatic amino acid transaminase involved in several otherwise unrelated metabolic pathways. Responsible for phenylalanine and tyrosine biosynthesis. Active with glutamate, phenylalanine, tyrosine and tryptophan as amino donors and with phenylpyruvate, hydroxyphenylpyruvate, 2-oxoglutarate and pyruvate as amino acceptors. Also active with methionine, alpha-aminoadipate and leucine as amino donors when phenylpyruvate is the amino acceptor and in the reverse reactions with the corresponding oxo acids and phenylalanine as amino donor. Catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage pathway primarily using aromatic amino acids (tyrosine, phenylalanine and tryptophan) as the amino donors. Catalyzes the formation of alpha-aminoadipate from alpha-ketoadipate in the lysine biosyntheic pathway..
Protein Sequence MTLPESKDFSYLFSDETNARKPSPLKTCIHLFQDPNIIFLGGGLPLKDYFPWDNLSVDSPKPPFPQGIGAPIDEQNCIKYTVNKDYADKSANPSNDIPLSRALQYGFSAGQPELLNFIRDHTKIIHDLKYKDWDVLATAGNTNAWESTLRVFCNRGDVILVEAHSFSSSLASAEAQGVITFPVPIDADGIIPEKLAKVMENWTPGAPKPKLLYTIPTGQNPTGTSIADHRKEAIYKIAQKYDFLIVEDEPYYFLQMNPYIKDLKEREKAQSSPKQDHDEFLKSLANTFLSLDTEGRVIRMDSFSKVLAPGTRLGWITGSSKILKPYLSLHEMTIQAPAGFTQVLVNATLSRWGQKGYLDWLLGLRHEYTLKRDCAIDALYKYLPQSDAFVINPPIAGMFFTVNIDASVHPEFKTKYNSDPYQLEQSLYHKVVERGVLVVPGSWFKSEGETEPPQPAESKEVSNPNIIFFRGTYAAVSPEKLTEGLKRLGDTLYEEFGISK
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
10PhosphorylationLPESKDFSYLFSDET
CCCCCCCCCCCCCCC		30.9322369663
11PhosphorylationPESKDFSYLFSDETN
CCCCCCCCCCCCCCC		16.2622369663
14PhosphorylationKDFSYLFSDETNARK
CCCCCCCCCCCCCCC		31.7622369663
17PhosphorylationSYLFSDETNARKPSP
CCCCCCCCCCCCCCC		38.8922369663
23PhosphorylationETNARKPSPLKTCIH
CCCCCCCCCCCHHHH		45.9925521595
56PhosphorylationYFPWDNLSVDSPKPP
CCCCCCCCCCCCCCC		30.0820377248
59PhosphorylationWDNLSVDSPKPPFPQ
CCCCCCCCCCCCCCC		32.4428132839
84SuccinylationCIKYTVNKDYADKSA
CEEEEECHHHCCCCC		48.0223954790
84AcetylationCIKYTVNKDYADKSA
CEEEEECHHHCCCCC		48.0224489116
89UbiquitinationVNKDYADKSANPSND
ECHHHCCCCCCCCCC		43.2123749301
89AcetylationVNKDYADKSANPSND
ECHHHCCCCCCCCCC		43.2124489116
94PhosphorylationADKSANPSNDIPLSR
CCCCCCCCCCCCHHH		47.1122369663
100PhosphorylationPSNDIPLSRALQYGF
CCCCCCHHHHHHHCC		15.3422369663
123AcetylationNFIRDHTKIIHDLKY
HHHHHHCHHHHCCCC		35.9222865919
129AcetylationTKIIHDLKYKDWDVL
CHHHHCCCCCCCEEE		57.2022865919
131AcetylationIIHDLKYKDWDVLAT
HHHCCCCCCCEEEEE		51.2424489116
213PhosphorylationAPKPKLLYTIPTGQN
CCCCCEEEEECCCCC		17.0422369663
214PhosphorylationPKPKLLYTIPTGQNP
CCCCEEEEECCCCCC		22.0522369663
217PhosphorylationKLLYTIPTGQNPTGT
CEEEEECCCCCCCCC		47.7722369663
222PhosphorylationIPTGQNPTGTSIADH
ECCCCCCCCCCHHHH		61.7222369663
224PhosphorylationTGQNPTGTSIADHRK
CCCCCCCCCHHHHHH		21.3122369663
225PhosphorylationGQNPTGTSIADHRKE
CCCCCCCCHHHHHHH		19.6822369663
236AcetylationHRKEAIYKIAQKYDF
HHHHHHHHHHHHCCE		26.0025381059
271PhosphorylationKEREKAQSSPKQDHD
HHHHHHHCCCCCCHH		54.1722369663
272PhosphorylationEREKAQSSPKQDHDE
HHHHHHCCCCCCHHH		24.8422369663
283PhosphorylationDHDEFLKSLANTFLS
CHHHHHHHHHHHHHC		34.5622369663
287PhosphorylationFLKSLANTFLSLDTE
HHHHHHHHHHCCCCC		21.9822369663
290PhosphorylationSLANTFLSLDTEGRV
HHHHHHHCCCCCCCE		21.7322369663
293PhosphorylationNTFLSLDTEGRVIRM
HHHHCCCCCCCEEEE		45.7022369663
305UbiquitinationIRMDSFSKVLAPGTR
EEECCCCCCCCCCCE		38.9824961812
305AcetylationIRMDSFSKVLAPGTR
EEECCCCCCCCCCCE		38.9824489116
311PhosphorylationSKVLAPGTRLGWITG
CCCCCCCCEEEEEEC		22.9728889911
317PhosphorylationGTRLGWITGSSKILK
CCEEEEEECCCCCHH		25.2221440633
326PhosphorylationSSKILKPYLSLHEMT
CCCCHHHHHEEEEEE		13.8222369663
328PhosphorylationKILKPYLSLHEMTIQ
CCHHHHHEEEEEEEE		23.1022369663
333PhosphorylationYLSLHEMTIQAPAGF
HHEEEEEEEECCCCH		13.6222369663
341PhosphorylationIQAPAGFTQVLVNAT
EECCCCHHHHHHHHH		19.4922369663
348PhosphorylationTQVLVNATLSRWGQK
HHHHHHHHHHHHCHH		21.7722369663
350PhosphorylationVLVNATLSRWGQKGY
HHHHHHHHHHCHHHH		22.9522369663
371SuccinylationLRHEYTLKRDCAIDA
CCCCHHHHCHHHHHH		38.0923954790
3712-HydroxyisobutyrylationLRHEYTLKRDCAIDA
CCCCHHHHCHHHHHH		38.09-
371AcetylationLRHEYTLKRDCAIDA
CCCCHHHHCHHHHHH		38.0922865919
415AcetylationVHPEFKTKYNSDPYQ
ECHHHHHCCCCCHHH		42.9224489116
430AcetylationLEQSLYHKVVERGVL
HHHHHHHHHHHCCEE		34.1224489116
430UbiquitinationLEQSLYHKVVERGVL
HHHHHHHHHHHCCEE		34.1223749301
445AcetylationVVPGSWFKSEGETEP
EEECCCCCCCCCCCC		41.1424489116
445UbiquitinationVVPGSWFKSEGETEP
EEECCCCCCCCCCCC		41.1423749301
459AcetylationPPQPAESKEVSNPNI
CCCCCCCCCCCCCCE		54.3524489116
477PhosphorylationRGTYAAVSPEKLTEG
ECCEEECCHHHHHHH		23.7128889911
480AcetylationYAAVSPEKLTEGLKR
EEECCHHHHHHHHHH		65.1824489116
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 ARO8_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARO8_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 ARO8_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARO9_YEASTARO9genetic
18625006
HSP7F_YEASTSSE1physical
19536198
ARO8_YEASTARO8physical
19343713
ARO9_YEASTARO9genetic
9491082
ACON2_YEASTACO2genetic
21623372
THRC_YEASTTHR4genetic
21623372
ALAM_YEASTALT1genetic
21623372
FOLE_YEASTMET7genetic
21623372
ADH3_YEASTADH3genetic
21623372
ERG2_YEASTERG2genetic
21623372
ARO8_YEASTARO8physical
23893908
ARO10_YEASTARO10genetic
25743068
ARO10_YEASTARO10genetic
25681107
GPR1_YEASTGPR1genetic
27708008
YMC2_YEASTYMC2genetic
27708008
CLPX_YEASTMCX1genetic
27708008
TXTP_YEASTCTP1genetic
27708008
THRC_YEASTTHR4genetic
27708008
VAM6_YEASTVAM6genetic
27708008
YD183_YEASTYDL183Cgenetic
27708008
UME6_YEASTUME6genetic
27708008
ALAM_YEASTALT1genetic
27708008
YHM2_YEASTYHM2genetic
27708008
FRE7_YEASTFRE7genetic
27708008
YEY2_YEASTYER152Cgenetic
28939805
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARO8_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-56; SER-100; SER-272 ANDSER-477, 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-271, AND MASSSPECTROMETRY.

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