KAR_YEAST - dbPTM
KAR_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KAR_YEAST
UniProt AC Q07551
Protein Name NADPH-dependent alpha-keto amide reductase
Gene Name YDL124W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 312
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Reduces aromatic alpha-keto amides, aliphatic and aromatic alpha-keto esters, but not beta-keto esters..
Protein Sequence MSFHQQFFTLNNGNKIPAIAIIGTGTRWYKNEETDATFSNSLVEQIVYALKLPGIIHIDAAEIYRTYPEVGKALSLTEKPRNAIFLTDKYSPQIKMSDSPADGLDLALKKMGTDYVDLYLLHSPFVSKEVNGLSLEEAWKDMEQLYKSGKAKNIGVSNFAVEDLQRILKVAEVKPQVNQIEFSPFLQNQTPGIYKFCQEHDILVEAYSPLGPLQKKTAQDDSQPFFEYVKELSEKYIKSEAQIILRWVTKRGVLPVTTSSKPQRISDAQNLFSFDLTAEEVDKITELGLEHEPLRLYWNKLYGKYNYAAQKV
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------MSFHQQFFT
------CCCCCCEEE		31.2822369663
9PhosphorylationSFHQQFFTLNNGNKI
CCCCCEEECCCCCCC		29.8422369663
24PhosphorylationPAIAIIGTGTRWYKN
CEEEEEECCCCCCCC		25.6022369663
26PhosphorylationIAIIGTGTRWYKNEE
EEEEECCCCCCCCCC		20.1922369663
72AcetylationRTYPEVGKALSLTEK
HHCHHHHHHCCCCCC		51.8624489116
72UbiquitinationRTYPEVGKALSLTEK
HHCHHHHHHCCCCCC		51.8617644757
75PhosphorylationPEVGKALSLTEKPRN
HHHHHHCCCCCCCCC		37.8023749301
77PhosphorylationVGKALSLTEKPRNAI
HHHHCCCCCCCCCEE		38.2921440633
79UbiquitinationKALSLTEKPRNAIFL
HHCCCCCCCCCEEEE		44.0017644757
87PhosphorylationPRNAIFLTDKYSPQI
CCCEEEECCCCCCCC		21.5022369663
89AcetylationNAIFLTDKYSPQIKM
CEEEECCCCCCCCCC		42.2524489116
89UbiquitinationNAIFLTDKYSPQIKM
CEEEECCCCCCCCCC		42.2523749301
90PhosphorylationAIFLTDKYSPQIKMS
EEEECCCCCCCCCCC		28.5222369663
91PhosphorylationIFLTDKYSPQIKMSD
EEECCCCCCCCCCCC		18.9722369663
97PhosphorylationYSPQIKMSDSPADGL
CCCCCCCCCCCCCHH		29.9024961812
99PhosphorylationPQIKMSDSPADGLDL
CCCCCCCCCCCHHHH		18.0622369663
109AcetylationDGLDLALKKMGTDYV
CHHHHHHHHHCCCCE		34.8024489116
123PhosphorylationVDLYLLHSPFVSKEV
EEEEEECCCCCCHHC		21.7217330950
152UbiquitinationLYKSGKAKNIGVSNF
HHHHCCCCCCCCCCH		53.2117644757
169UbiquitinationEDLQRILKVAEVKPQ
HHHHHHHHHHHCCCC		36.7117644757
174UbiquitinationILKVAEVKPQVNQIE
HHHHHHCCCCCCEEE		22.6517644757
174AcetylationILKVAEVKPQVNQIE
HHHHHHCCCCCCEEE		22.6524489116
195UbiquitinationNQTPGIYKFCQEHDI
CCCCCHHHHHHHCCE		37.4317644757
215AcetylationSPLGPLQKKTAQDDS
CCCCHHCCCCCCCCC		60.8324489116
230AcetylationQPFFEYVKELSEKYI
CHHHHHHHHHHHHHH		52.6224489116
235AcetylationYVKELSEKYIKSEAQ
HHHHHHHHHHHHHHH		49.2322865919
238UbiquitinationELSEKYIKSEAQIIL
HHHHHHHHHHHHHHH		38.8723749301
261AcetylationLPVTTSSKPQRISDA
EEEECCCCCCCCCCC		44.9624489116
300AcetylationPLRLYWNKLYGKYNY
CHHHHHHHHHCHHHH		29.0124489116
304AcetylationYWNKLYGKYNYAAQK
HHHHHHCHHHHHCCC		19.4324489116
311SuccinylationKYNYAAQKV------
HHHHHCCCC------		45.2223954790
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 KAR_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KAR_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 KAR_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASH1_YEASTASH1physical
20844764
STB5_YEASTSTB5genetic
27708008
YNB1_YEASTYNL011Cgenetic
27708008
PSB6_YEASTPRE7genetic
27708008
ACT_YEASTACT1genetic
27708008
GPI10_YEASTGPI10genetic
27708008
YIP1_YEASTYIP1genetic
27708008
MED6_YEASTMED6genetic
27708008
FNTA_YEASTRAM2genetic
27708008
SEC39_YEASTSEC39genetic
27708008
MCM1_YEASTMCM1genetic
27708008
LCB1_YEASTLCB1genetic
27708008
DBP6_YEASTDBP6genetic
27708008
NUF2_YEASTNUF2genetic
27708008
DIM1_YEASTDIM1genetic
27708008
DIB1_YEASTDIB1genetic
27708008
MED10_YEASTNUT2genetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
PRM9_YEASTPRM9genetic
27708008
FMT_YEASTFMT1genetic
27708008
ADPP_YEASTYSA1genetic
27708008
BUD31_YEASTBUD31genetic
27708008
STB3_YEASTSTB3genetic
27708008
DPP1_YEASTDPP1genetic
27708008
APA2_YEASTAPA2genetic
27708008
KCC1_YEASTCMK1genetic
27708008
RL24A_YEASTRPL24Agenetic
27708008
YGI1_YEASTYGL081Wgenetic
27708008
DBF2_YEASTDBF2genetic
27708008
KEL2_YEASTKEL2genetic
27708008
SAY1_YEASTSAY1genetic
27708008
OCA5_YEASTOCA5genetic
27708008
MED20_YEASTSRB2genetic
27708008
MPC2_YEASTMPC2genetic
27708008
ACA2_YEASTCST6genetic
27708008
ASF1_YEASTASF1genetic
27708008
3HAO_YEASTBNA1genetic
27708008
ILM1_YEASTILM1genetic
27708008
MRT4_YEASTMRT4genetic
27708008
SAC1_YEASTSAC1genetic
27708008
FKS1_YEASTFKS1genetic
27708008
DIA1_YEASTDIA1genetic
27708008
TOM70_YEASTTOM70genetic
27708008
ESBP6_YEASTESBP6genetic
27708008
DUS2_YEASTSMM1genetic
27708008
HUB1_YEASTHUB1genetic
27708008
DCAM_YEASTSPE2genetic
27708008
INO4_YEASTINO4genetic
27708008
GAS4_YEASTGAS4genetic
27708008
PUR6_YEASTADE2genetic
27708008
IES4_YEASTIES4genetic
27708008
RAD1_YEASTRAD1genetic
27708008
SVL3_YEASTSVL3genetic
27708008
MRX11_YEASTYPL041Cgenetic
27708008
POC4_YEASTPOC4genetic
27708008
BEM4_YEASTBEM4genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KAR_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-123, AND MASSSPECTROMETRY.

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