ARO10_YEAST - dbPTM
ARO10_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARO10_YEAST
UniProt AC Q06408
Protein Name Transaminated amino acid decarboxylase
Gene Name ARO10
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 635
Subcellular Localization Cytoplasm .
Protein Description One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-acids). In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from phenylalanine (phenylpyruvate), tryptophan (3-(indol-3-yl)pyruvate), and probably tyrosine (4-hydroxyphenylpyruvate), but also isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate) and methionine (4-methylthio-2-oxobutanoate), whereas transaminated leucine (4-methyl-2-oxopentanoate, also alpha-keto-isocaproate) is a low efficiency substrate and transaminated valine and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins..
Protein Sequence MAPVTIEKFVNQEERHLVSNRSATIPFGEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYSPSVESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSALNGIAGSFAENVKVLHIVGVAKSIDSRSSNFSDRNLHHLVPQLHDSNFKGPNHKVYHDMVKDRVACSVAYLEDIETACDQVDNVIRDIYKYSKPGYIFVPADFADMSVTCDNLVNVPRISQQDCIVYPSENQLSDIINKITSWIYSSKTPAILGDVLTDRYGVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYNGKEGLKQVYEHFELCDLVLHFGVDINEINNGHYTFTYKPNAKIIQFHPNYIRLVDTRQGNEQMFKGINFAPILKELYKRIDVSKLSLQYDSNVTQYTNETMRLEDPTNGQSSIITQVHLQKTMPKFLNPGDVVVCETGSFQFSVRDFAFPSQLKYISQGFFLSIGMALPAALGVGIAMQDHSNAHINGGNVKEDYKPRLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGYTIERAIMGPTRSYNDVMSWKWTKLFEAFGDFDGKYTNSTLIQCPSKLALKLEELKNSNKRSGIELLEVKLGELDFPEQLKCMVEAAALKRNKK
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
33AcetylationPFGEYIFKRLLSIDT
CCHHHHHHHHHCCCC		32.3622865919
59PhosphorylationLSLLEYLYSPSVESA
HHHHHHHHCCCCHHC		20.0327017623
60PhosphorylationSLLEYLYSPSVESAG
HHHHHHHCCCCHHCC		14.2227017623
65PhosphorylationLYSPSVESAGLRWVG
HHCCCCHHCCCEEEE		26.0227017623
129AcetylationLHIVGVAKSIDSRSS
EEEEEEEECCCCCCC		45.6022865919
168AcetylationKVYHDMVKDRVACSV
CCCHHHHHHHCHHEH		32.9322865919
197UbiquitinationNVIRDIYKYSKPGYI
HHHHHHHHHCCCCEE		43.3015699485
357PhosphorylationIIQFHPNYIRLVDTR
EEEECCCEEEEEECC		7.5922369663
372UbiquitinationQGNEQMFKGINFAPI
CCCHHHHCCCCHHHH		54.2418433149
381UbiquitinationINFAPILKELYKRID
CCHHHHHHHHHHHCC		46.5215699485
527UbiquitinationQELSTILKCNIPLEV
HHHHHHHCCCCCEEE		22.7615699485
577PhosphorylationFGDFDGKYTNSTLIQ
HCCCCCCCCCCEEEE		19.3827214570
578PhosphorylationGDFDGKYTNSTLIQC
CCCCCCCCCCEEEEC		26.6127214570
580PhosphorylationFDGKYTNSTLIQCPS
CCCCCCCCEEEECCC		19.4527214570
581PhosphorylationDGKYTNSTLIQCPSK
CCCCCCCEEEECCCH		29.9227214570
588AcetylationTLIQCPSKLALKLEE
EEEECCCHHHHHHHH		23.9522865919
588UbiquitinationTLIQCPSKLALKLEE
EEEECCCHHHHHHHH		23.9522817900
592UbiquitinationCPSKLALKLEELKNS
CCCHHHHHHHHHHCC		48.5222817900
597UbiquitinationALKLEELKNSNKRSG
HHHHHHHHCCCCCCC		62.7022817900
611UbiquitinationGIELLEVKLGELDFP
CEEEEEEECCCCCCH		41.2015699485
622UbiquitinationLDFPEQLKCMVEAAA
CCCHHHHHHHHHHHH		21.7015699485
631UbiquitinationMVEAAALKRNKK---
HHHHHHHHHHCC---		49.5515699485
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 ARO10_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARO10_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 ARO10_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAPZB_YEASTCAP2physical
18467557
EMC5_YEASTEMC5physical
18467557
POS5_YEASTPOS5genetic
21623372
OYE2_YEASTOYE2physical
22940862
ARO10_YEASTARO10physical
22940862
BCA1_YEASTBAT1genetic
26721212
CLP1_YEASTCLP1genetic
27708008
CDC24_YEASTCDC24genetic
27708008
KPC1_YEASTPKC1genetic
27708008
CALM_YEASTCMD1genetic
27708008
PRP9_YEASTPRP9genetic
27708008
RPN6_YEASTRPN6genetic
27708008
DPOD_YEASTPOL3genetic
27708008
RSP5_YEASTRSP5genetic
27708008
SWC4_YEASTSWC4genetic
27708008
MPPA_YEASTMAS2genetic
27708008
MET30_YEASTMET30genetic
27708008
KTHY_YEASTCDC8genetic
27708008
SEC22_YEASTSEC22genetic
27708008
TYSY_YEASTCDC21genetic
27708008
EI2BG_YEASTGCD1genetic
27708008
PMP1_YEASTPMP1physical
26404137
EFC14_HUMANEFCAB14physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARO10_YEAST

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Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-588, AND MASSSPECTROMETRY.

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