PDC1_YEAST - dbPTM
PDC1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDC1_YEAST
UniProt AC P06169
Protein Name Pyruvate decarboxylase isozyme 1
Gene Name PDC1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 563
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Major of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-ketoacids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo 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 threonine (2-oxobutanoate), norvaline (2-oxopentanoate), valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate), isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins..
Protein Sequence MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISAQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQRPVYLGLPANLVDLNVPAKLLQTPIDMSLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVTPMGKGSIDEQHPRYGGVYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIRNATFPGVQMKFVLQKLLTTIADAAKGYKPVAVPARTPANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAAEEIDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGPKAQYNEIQGWDHLSLLPTFGAKDYETHRVATTGEWDKLTQDKSFNDNSKIRMIEIMLPVFDAPQNLVEQAKLTAATNAKQ
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
2Acetylation------MSEITLGKY
------CCCCHHHHH		37.399298649
2Phosphorylation------MSEITLGKY
------CCCCHHHHH		37.3928152593
5Phosphorylation---MSEITLGKYLFE
---CCCCHHHHHHHH		25.9619823750
82-HydroxyisobutyrylationMSEITLGKYLFERLK
CCCCHHHHHHHHHHH		41.72-
8AcetylationMSEITLGKYLFERLK
CCCCHHHHHHHHHHH		41.7224489116
8SuccinylationMSEITLGKYLFERLK
CCCCHHHHHHHHHHH		41.7223954790
8UbiquitinationMSEITLGKYLFERLK
CCCCHHHHHHHHHHH		41.7224961812
9PhosphorylationSEITLGKYLFERLKQ
CCCHHHHHHHHHHHC		18.1521440633
36UbiquitinationFNLSLLDKIYEVEGM
CCHHHHHHHEEECCC		47.3515699485
129PhosphorylationFTVFHRMSANISETT
EEEEEEEECCCCCCE		20.3722369663
133PhosphorylationHRMSANISETTAMIT
EEEECCCCCCEEEEE		28.7919779198
135PhosphorylationMSANISETTAMITDI
EECCCCCCEEEEEHH		17.0522369663
136PhosphorylationSANISETTAMITDIA
ECCCCCCEEEEEHHH		15.3522369663
140PhosphorylationSETTAMITDIATAPA
CCCEEEEEHHHCCHH		14.3122369663
144PhosphorylationAMITDIATAPAEIDR
EEEEHHHCCHHHHHH		33.2419779198
155PhosphorylationEIDRCIRTTYVTQRP
HHHHHHCCEECCCCC		11.5428889911
156PhosphorylationIDRCIRTTYVTQRPV
HHHHHCCEECCCCCE		13.2229688323
157PhosphorylationDRCIRTTYVTQRPVY
HHHHCCEECCCCCEE		10.8221440633
159PhosphorylationCIRTTYVTQRPVYLG
HHCCEECCCCCEECC		14.4021440633
164PhosphorylationYVTQRPVYLGLPANL
ECCCCCEECCCCCCC		9.5729688323
179UbiquitinationVDLNVPAKLLQTPID
CCCCCCHHHHCCCCC		43.5924961812
183PhosphorylationVPAKLLQTPIDMSLK
CCHHHHCCCCCCCCC		23.3722369663
188PhosphorylationLQTPIDMSLKPNDAE
HCCCCCCCCCCCCHH		29.5022369663
1902-HydroxyisobutyrylationTPIDMSLKPNDAESE
CCCCCCCCCCCHHHH		34.17-
190AcetylationTPIDMSLKPNDAESE
CCCCCCCCCCCHHHH		34.1724489116
190SuccinylationTPIDMSLKPNDAESE
CCCCCCCCCCCHHHH		34.1723954790
190UbiquitinationTPIDMSLKPNDAESE
CCCCCCCCCCCHHHH		34.1723749301
196PhosphorylationLKPNDAESEKEVIDT
CCCCCHHHHHHHHHH		56.5422369663
198SuccinylationPNDAESEKEVIDTIL
CCCHHHHHHHHHHHH		67.5723954790
198UbiquitinationPNDAESEKEVIDTIL
CCCHHHHHHHHHHHH		67.5723749301
203PhosphorylationSEKEVIDTILALVKD
HHHHHHHHHHHHHHC		13.5319795423
209AcetylationDTILALVKDAKNPVI
HHHHHHHHCCCCCEE		53.4724489116
209SuccinylationDTILALVKDAKNPVI
HHHHHHHHCCCCCEE		53.4723954790
209UbiquitinationDTILALVKDAKNPVI
HHHHHHHHCCCCCEE		53.4724961812
212AcetylationLALVKDAKNPVILAD
HHHHHCCCCCEEEEE		72.4324489116
212UbiquitinationLALVKDAKNPVILAD
HHHHHCCCCCEEEEE		72.4323749301
223PhosphorylationILADACCSRHDVKAE
EEEEHHCCCCCCCHH		32.3122369663
2282-HydroxyisobutyrylationCCSRHDVKAETKKLI
HCCCCCCCHHHHHHH		46.71-
228AcetylationCCSRHDVKAETKKLI
HCCCCCCCHHHHHHH		46.7124489116
228SuccinylationCCSRHDVKAETKKLI
HCCCCCCCHHHHHHH		46.7123954790
228UbiquitinationCCSRHDVKAETKKLI
HCCCCCCCHHHHHHH		46.7122817900
232UbiquitinationHDVKAETKKLIDLTQ
CCCCHHHHHHHHHHH		36.7722817900
2332-HydroxyisobutyrylationDVKAETKKLIDLTQF
CCCHHHHHHHHHHHC		59.08-
233AcetylationDVKAETKKLIDLTQF
CCCHHHHHHHHHHHC		59.0824489116
233UbiquitinationDVKAETKKLIDLTQF
CCCHHHHHHHHHHHC		59.0823749301
238PhosphorylationTKKLIDLTQFPAFVT
HHHHHHHHHCCEEEC		25.1522369663
245PhosphorylationTQFPAFVTPMGKGSI
HHCCEEECCCCCCCC		10.9122369663
249AcetylationAFVTPMGKGSIDEQH
EEECCCCCCCCCCCC		43.1424489116
249SuccinylationAFVTPMGKGSIDEQH
EEECCCCCCCCCCCC		43.1423954790
249UbiquitinationAFVTPMGKGSIDEQH
EEECCCCCCCCCCCC		43.1423749301
251PhosphorylationVTPMGKGSIDEQHPR
ECCCCCCCCCCCCCC		30.2821440633
259PhosphorylationIDEQHPRYGGVYVGT
CCCCCCCCCEEEEEC		23.7621440633
263PhosphorylationHPRYGGVYVGTLSKP
CCCCCEEEEECCCCH		9.0922369663
266PhosphorylationYGGVYVGTLSKPEVK
CCEEEEECCCCHHHH		20.1522369663
268PhosphorylationGVYVGTLSKPEVKEA
EEEEECCCCHHHHHH		46.1020377248
2692-HydroxyisobutyrylationVYVGTLSKPEVKEAV
EEEECCCCHHHHHHH		48.59-
269AcetylationVYVGTLSKPEVKEAV
EEEECCCCHHHHHHH		48.5924489116
269SuccinylationVYVGTLSKPEVKEAV
EEEECCCCHHHHHHH		48.5923954790
269UbiquitinationVYVGTLSKPEVKEAV
EEEECCCCHHHHHHH		48.5923749301
273UbiquitinationTLSKPEVKEAVESAD
CCCCHHHHHHHHHCC		37.9922817900
294PhosphorylationALLSDFNTGSFSYSY
HHHHCCCCCCCCCEE		33.9128889911
296PhosphorylationLSDFNTGSFSYSYKT
HHCCCCCCCCCEEEC		14.6928889911
300PhosphorylationNTGSFSYSYKTKNIV
CCCCCCCEEECCCEE		20.9627214570
302UbiquitinationGSFSYSYKTKNIVEF
CCCCCEEECCCEEEE		47.2722817900
3042-HydroxyisobutyrylationFSYSYKTKNIVEFHS
CCCEEECCCEEEEEC		40.29-
304AcetylationFSYSYKTKNIVEFHS
CCCEEECCCEEEEEC		40.2922865919
304SuccinylationFSYSYKTKNIVEFHS
CCCEEECCCEEEEEC		40.2923954790
304UbiquitinationFSYSYKTKNIVEFHS
CCCEEECCCEEEEEC		40.2923749301
311PhosphorylationKNIVEFHSDHMKIRN
CCEEEEECCCCCHHC		34.2321440633
3152-HydroxyisobutyrylationEFHSDHMKIRNATFP
EEECCCCCHHCCCCC		34.78-
315AcetylationEFHSDHMKIRNATFP
EEECCCCCHHCCCCC		34.7824489116
315SuccinylationEFHSDHMKIRNATFP
EEECCCCCHHCCCCC		34.7823954790
315UbiquitinationEFHSDHMKIRNATFP
EEECCCCCHHCCCCC		34.7823749301
320PhosphorylationHMKIRNATFPGVQMK
CCCHHCCCCCCHHHH		33.6322369663
3272-HydroxyisobutyrylationTFPGVQMKFVLQKLL
CCCCHHHHHHHHHHH		18.41-
327AcetylationTFPGVQMKFVLQKLL
CCCCHHHHHHHHHHH		18.4124489116
3322-HydroxyisobutyrylationQMKFVLQKLLTTIAD
HHHHHHHHHHHHHHH		41.10-
332AcetylationQMKFVLQKLLTTIAD
HHHHHHHHHHHHHHH		41.1024489116
332UbiquitinationQMKFVLQKLLTTIAD
HHHHHHHHHHHHHHH		41.1023749301
335PhosphorylationFVLQKLLTTIADAAK
HHHHHHHHHHHHHHC		26.9620377248
336PhosphorylationVLQKLLTTIADAAKG
HHHHHHHHHHHHHCC		17.7120377248
3422-HydroxyisobutyrylationTTIADAAKGYKPVAV
HHHHHHHCCCCCEEE		65.57-
342AcetylationTTIADAAKGYKPVAV
HHHHHHHCCCCCEEE		65.5724489116
342SuccinylationTTIADAAKGYKPVAV
HHHHHHHCCCCCEEE		65.5723954790
342UbiquitinationTTIADAAKGYKPVAV
HHHHHHHCCCCCEEE		65.5723749301
344PhosphorylationIADAAKGYKPVAVPA
HHHHHCCCCCEEECC		16.0621440633
3452-HydroxyisobutyrylationADAAKGYKPVAVPAR
HHHHCCCCCEEECCC		41.50-
345AcetylationADAAKGYKPVAVPAR
HHHHCCCCCEEECCC		41.5024489116
345SuccinylationADAAKGYKPVAVPAR
HHHHCCCCCEEECCC		41.5023954790
345UbiquitinationADAAKGYKPVAVPAR
HHHHCCCCCEEECCC		41.5023749301
353PhosphorylationPVAVPARTPANAAVP
CEEECCCCCCCCCCC		28.9422369663
362PhosphorylationANAAVPASTPLKQEW
CCCCCCCCCCCCHHH		25.2022369663
363PhosphorylationNAAVPASTPLKQEWM
CCCCCCCCCCCHHHH		34.4422369663
366UbiquitinationVPASTPLKQEWMWNQ
CCCCCCCCHHHHHHH		47.5817644757
463AcetylationTMIRWGLKPYLFVLN
HHHHCCCCCEEEEEC		27.9024489116
463SuccinylationTMIRWGLKPYLFVLN
HHHHCCCCCEEEEEC		27.9023954790
463UbiquitinationTMIRWGLKPYLFVLN
HHHHCCCCCEEEEEC		27.9023749301
478AcetylationNDGYTIEKLIHGPKA
CCCCEEHHHHCCCHH		49.2224489116
478UbiquitinationNDGYTIEKLIHGPKA
CCCCEEHHHHCCCHH		49.2217644757
484AcetylationEKLIHGPKAQYNEIQ
HHHHCCCHHHCCCCC		53.3524489116
484UbiquitinationEKLIHGPKAQYNEIQ
HHHHCCCHHHCCCCC		53.3523749301
487PhosphorylationIHGPKAQYNEIQGWD
HCCCHHHCCCCCCCC		21.4421440633
497PhosphorylationIQGWDHLSLLPTFGA
CCCCCEEECCCCCCC		25.1721440633
501PhosphorylationDHLSLLPTFGAKDYE
CEEECCCCCCCCCCC		34.3722369663
5052-HydroxyisobutyrylationLLPTFGAKDYETHRV
CCCCCCCCCCCCEEE		62.31-
505AcetylationLLPTFGAKDYETHRV
CCCCCCCCCCCCEEE		62.3124489116
505UbiquitinationLLPTFGAKDYETHRV
CCCCCCCCCCCCEEE		62.3123749301
509PhosphorylationFGAKDYETHRVATTG
CCCCCCCCEEEECCC		14.5717287358
514PhosphorylationYETHRVATTGEWDKL
CCCEEEECCCCHHHH		32.2622369663
515PhosphorylationETHRVATTGEWDKLT
CCEEEECCCCHHHHC		24.3029136822
5202-HydroxyisobutyrylationATTGEWDKLTQDKSF
ECCCCHHHHCCCCCC		55.28-
520AcetylationATTGEWDKLTQDKSF
ECCCCHHHHCCCCCC		55.2824489116
520SuccinylationATTGEWDKLTQDKSF
ECCCCHHHHCCCCCC		55.2823954790
520UbiquitinationATTGEWDKLTQDKSF
ECCCCHHHHCCCCCC		55.2823749301
522PhosphorylationTGEWDKLTQDKSFND
CCCHHHHCCCCCCCC		40.2328889911
5252-HydroxyisobutyrylationWDKLTQDKSFNDNSK
HHHHCCCCCCCCCCC		47.32-
525AcetylationWDKLTQDKSFNDNSK
HHHHCCCCCCCCCCC		47.3224489116
525SuccinylationWDKLTQDKSFNDNSK
HHHHCCCCCCCCCCC		47.3223954790
525UbiquitinationWDKLTQDKSFNDNSK
HHHHCCCCCCCCCCC		47.3223749301
526PhosphorylationDKLTQDKSFNDNSKI
HHHCCCCCCCCCCCE		37.2625521595
531PhosphorylationDKSFNDNSKIRMIEI
CCCCCCCCCEEEEEE		32.1221440633
5322-HydroxyisobutyrylationKSFNDNSKIRMIEIM
CCCCCCCCEEEEEEE		40.35-
532AcetylationKSFNDNSKIRMIEIM
CCCCCCCCEEEEEEE		40.3524489116
532SuccinylationKSFNDNSKIRMIEIM
CCCCCCCCEEEEEEE		40.3523954790
532UbiquitinationKSFNDNSKIRMIEIM
CCCCCCCCEEEEEEE		40.3523749301
554AcetylationQNLVEQAKLTAATNA
HHHHHHHHHHHHHCC		46.1724489116
554SuccinylationQNLVEQAKLTAATNA
HHHHHHHHHHHHHCC		46.1723954790
554UbiquitinationQNLVEQAKLTAATNA
HHHHHHHHHHHHHCC		46.1724961812
556PhosphorylationLVEQAKLTAATNAKQ
HHHHHHHHHHHCCCC		17.3428889911
559PhosphorylationQAKLTAATNAKQ---
HHHHHHHHCCCC---		32.9928889911
5622-HydroxyisobutyrylationLTAATNAKQ------
HHHHHCCCC------		59.62-
562AcetylationLTAATNAKQ------
HHHHHCCCC------		59.6224489116
562SuccinylationLTAATNAKQ------
HHHHHCCCC------		59.6223954790
562UbiquitinationLTAATNAKQ------
HHHHHCCCC------		59.6223749301
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 PDC1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDC1_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 PDC1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDC5_YEASTPDC5genetic
2185016
PDC5_YEASTPDC5genetic
9748245
PDC6_YEASTPDC6genetic
9748245
PDC5_YEASTPDC5genetic
1807827
MED3_YEASTPGD1genetic
17314980
SLX5_YEASTSLX5genetic
17314980
EAF1_YEASTEAF1genetic
17314980
MED2_YEASTMED2genetic
17314980
RPC8_YEASTRPC25genetic
17314980
MED5_YEASTNUT1genetic
17314980
RGP1_YEASTRGP1genetic
17314980
REI1_YEASTREI1genetic
17314980
PFD1_YEASTPFD1genetic
17314980
BMH1_YEASTBMH1genetic
17314980
PDC1_YEASTPDC1physical
8512926
PDC1_YEASTPDC1physical
10651824
PDC1_YEASTPDC1physical
19246454
PDC5_YEASTPDC5genetic
16941010
PDC6_YEASTPDC6genetic
16941010
NHP10_YEASTNHP10genetic
20093466
VMS1_YEASTVMS1genetic
20093466
XRS2_YEASTXRS2genetic
20093466
XRN1_YEASTXRN1genetic
20093466
PIB2_YEASTPIB2genetic
20093466
SNF6_YEASTSNF6genetic
20093466
THIK_YEASTPOT1genetic
20093466
ELF1_YEASTELF1genetic
20093466
PDC5_YEASTPDC5genetic
20093466
RAD52_YEASTRAD52genetic
20093466
SPP1_YEASTSPP1genetic
20093466
DBP1_YEASTDBP1genetic
20093466
BRR1_YEASTBRR1genetic
20093466
YP089_YEASTYPR089Wgenetic
20093466
CSG2_YEASTCSG2genetic
21623372
6PGD1_YEASTGND1genetic
21623372
CRD1_YEASTCRD1genetic
21623372
THRC_YEASTTHR4genetic
21623372
ATPK_YEASTATP17genetic
21623372
ADH3_YEASTADH3genetic
21623372
MTH1_YEASTMTH1genetic
22978798
PRP6_YEASTPRP6genetic
27708008
CDC24_YEASTCDC24genetic
27708008
FAD1_YEASTFAD1genetic
27708008
RPC10_YEASTRPC11genetic
27708008
PDC2_YEASTPDC2genetic
27708008
CDC4_YEASTCDC4genetic
27708008
GNA1_YEASTGNA1genetic
27708008
MED6_YEASTMED6genetic
27708008
SEC22_YEASTSEC22genetic
27708008
TAD3_YEASTTAD3genetic
27708008
VTI1_YEASTVTI1genetic
27708008
GPI12_YEASTGPI12genetic
27708008
SGT1_YEASTSGT1genetic
27708008
MED4_YEASTMED4genetic
27708008
BUR1_YEASTSGV1genetic
27708008
MED10_YEASTNUT2genetic
27708008
NHP10_YEASTNHP10genetic
27708008
VMS1_YEASTVMS1genetic
27708008
HSP78_YEASTHSP78genetic
27708008
XRS2_YEASTXRS2genetic
27708008
RV167_YEASTRVS167genetic
27708008
PIB2_YEASTPIB2genetic
27708008
XRN1_YEASTXRN1genetic
27708008
HXKB_YEASTHXK2genetic
27708008
SNF6_YEASTSNF6genetic
27708008
THIK_YEASTPOT1genetic
27708008
DHOM_YEASTHOM6genetic
27708008
AIM26_YEASTAIM26genetic
27708008
ALDH4_YEASTALD4genetic
27708008
LCL1_YEASTLCL1genetic
27708008
PDR12_YEASTPDR12genetic
27708008
DBP1_YEASTDBP1genetic
27708008
SPP1_YEASTSPP1genetic
27708008
VPS4_YEASTVPS4genetic
27708008
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PDC1_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Identification and specificities of N-terminal acetyltransferasesfrom Saccharomyces cerevisiae.";
Polevoda B., Norbeck J., Takakura H., Blomberg A., Sherman F.;
EMBO J. 18:6155-6168(1999).
Cited for: ACETYLATION AT SER-2.
"Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins.";
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.;
Electrophoresis 18:1347-1360(1997).
Cited for: ACETYLATION AT SER-2.
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-223; THR-266; THR-320;SER-362; THR-363 AND SER-526, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223 AND THR-353, ANDMASS 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 THR-509 AND THR-514, ANDMASS SPECTROMETRY.

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