AMPD_YEAST - dbPTM
AMPD_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMPD_YEAST
UniProt AC P15274
Protein Name AMP deaminase
Gene Name AMD1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 810
Subcellular Localization
Protein Description AMP deaminase plays a critical role in energy metabolism..
Protein Sequence MDNQATQRLNDLSLEPAPSHDEQDGSGLVIDIDQRKIGDEQAGVVVDDETPPLEQQDSHESLAADSRNANFSYHENQQLLENGTKQLALDEHDSHSAILEQPSHSTNCSSSNIAAMNKGHDSADHASQNSGGKPRTLSASAQHILPETLKSFAGAPVVNKQVRTSASYKMGMLADDASQQFLDDPSSELIDLYSKVAECRNLRAKYQTISVQNDDQNPKNKPGWVVYPPPPKPSYNSDTKTVVPVTNKPDAEVFDFTKCEIPGEDPDWEFTLNDDDSYVVHRSGKTDELIAQIPTLRDYYLDLEKMISISSDGPAKSFAYRRLQYLEARWNLYYLLNEYQETSVSKRNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKHKLRHSKDEKVIFRDGKLLTLDEVFRSLHLTGYDLSIDTLDMHAHKDTFHRFDKFNLKYNPIGESRLREIFLKTNNYIKGTYLADITKQVIFDLENSKYQNCEYRISVYGRSLDEWDKLASWVIDNKVISHNVRWLVQIPRLYDIYKKTGIVQSFQDICKNLFQPLFEVTKNPQSHPKLHVFLQRVIGFDSVDDESKVDRRFHRKYPKPSLWEAPQNPPYSYYLYYLYSNVASLNQWRAKRGFNTLVLRPHCGEAGDPEHLVSAYLLAHGISHGILLRKVPFVQYLYYLDQVGIAMSPLSNNALFLTYDKNPFPRYFKRGLNVSLSTDDPLQFSYTREPLIEEYSVAAQIYKLSNVDMCELARNSVLQSGWEAQIKKHWIGKDFDKSGVEGNDVVRTNVPDIRINYRYDTLSTELELVNHFANFKRTIEEK
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
13PhosphorylationTQRLNDLSLEPAPSH
HHHHHCCCCCCCCCC		33.2822369663
19PhosphorylationLSLEPAPSHDEQDGS
CCCCCCCCCCCCCCC		45.7522369663
26PhosphorylationSHDEQDGSGLVIDID
CCCCCCCCEEEEECC		36.9222369663
50PhosphorylationGVVVDDETPPLEQQD
CEEECCCCCCHHHCC		36.8822369663
58PhosphorylationPPLEQQDSHESLAAD
CCHHHCCCCHHHHHH		25.4722369663
61PhosphorylationEQQDSHESLAADSRN
HHCCCCHHHHHHHCC		20.2022369663
66PhosphorylationHESLAADSRNANFSY
CHHHHHHHCCCCCCH		23.7822369663
72PhosphorylationDSRNANFSYHENQQL
HHCCCCCCHHHHHHH		25.9530377154
73PhosphorylationSRNANFSYHENQQLL
HCCCCCCHHHHHHHH		14.7130377154
94PhosphorylationLALDEHDSHSAILEQ
EECCCCCCCCHHHCC		22.6519779198
96PhosphorylationLDEHDSHSAILEQPS
CCCCCCCCHHHCCCC		22.4321440633
103PhosphorylationSAILEQPSHSTNCSS
CHHHCCCCCCCCCCH		29.7521440633
105PhosphorylationILEQPSHSTNCSSSN
HHCCCCCCCCCCHHH		26.1720377248
106PhosphorylationLEQPSHSTNCSSSNI
HCCCCCCCCCCHHHH		34.5221440633
109PhosphorylationPSHSTNCSSSNIAAM
CCCCCCCCHHHHHHH		38.5821440633
110PhosphorylationSHSTNCSSSNIAAMN
CCCCCCCHHHHHHHH		29.6021440633
111PhosphorylationHSTNCSSSNIAAMNK
CCCCCCHHHHHHHHC		18.8921440633
122PhosphorylationAMNKGHDSADHASQN
HHHCCCCCCHHHHHC		29.8919823750
127PhosphorylationHDSADHASQNSGGKP
CCCCHHHHHCCCCCC		26.8619823750
130PhosphorylationADHASQNSGGKPRTL
CHHHHHCCCCCCCCC		41.0919823750
136PhosphorylationNSGGKPRTLSASAQH
CCCCCCCCCCHHHHH		33.3222369663
138PhosphorylationGGKPRTLSASAQHIL
CCCCCCCCHHHHHHC		21.4022369663
140PhosphorylationKPRTLSASAQHILPE
CCCCCCHHHHHHCHH		25.7022369663
148PhosphorylationAQHILPETLKSFAGA
HHHHCHHHHHHHCCC		37.2319823750
150UbiquitinationHILPETLKSFAGAPV
HHCHHHHHHHCCCCC		51.4517644757
167PhosphorylationKQVRTSASYKMGMLA
HHCCCCCCHHCCCCC		25.6721440633
178PhosphorylationGMLADDASQQFLDDP
CCCCCHHHHHHHCCC		31.3521440633
248AcetylationTVVPVTNKPDAEVFD
CEEECCCCCCCEEEC		34.6024489116
285UbiquitinationYVVHRSGKTDELIAQ
EEEECCCCCHHHHHH		54.7917644757
299PhosphorylationQIPTLRDYYLDLEKM
HCCCHHHHCCCHHHH		10.2525882841
300PhosphorylationIPTLRDYYLDLEKMI
CCCHHHHCCCHHHHH		9.6819779198
305UbiquitinationDYYLDLEKMISISSD
HHCCCHHHHHCCCCC		49.1617644757
308PhosphorylationLDLEKMISISSDGPA
CCHHHHHCCCCCCCH		16.9625882841
310PhosphorylationLEKMISISSDGPAKS
HHHHHCCCCCCCHHH		18.6519779198
317PhosphorylationSSDGPAKSFAYRRLQ
CCCCCHHHHHHHHHH		19.7419779198
320PhosphorylationGPAKSFAYRRLQYLE
CCHHHHHHHHHHHHH		8.3425882841
396AcetylationKVIFRDGKLLTLDEV
CEEEECCCEEEHHHH		44.6124489116
433AcetylationDTFHRFDKFNLKYNP
HHCCCCHHCCCCCCC		33.1824489116
477AcetylationIFDLENSKYQNCEYR
EEECCCCCCCCEEEE		63.5424489116
549PhosphorylationFQPLFEVTKNPQSHP
CHHHHHHCCCCCCCC		20.2221440633
554PhosphorylationEVTKNPQSHPKLHVF
HHCCCCCCCCCHHHH		42.9121440633
576AcetylationDSVDDESKVDRRFHR
CCCCCCHHHHHHHHH		46.2224489116
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 AMPD_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMPD_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 AMPD_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AMPD_YEASTAMD1physical
18467557
AMPD_YEASTAMD1physical
18719252
YB9Z_YEASTYBR284Wphysical
18719252
YJH0_YEASTYJL070Cphysical
18719252
ADH1_YEASTADH1genetic
15869715
6PGD1_YEASTGND1genetic
21623372
ADE_YEASTAAH1genetic
21623372
ELO2_YEASTELO2genetic
21623372
DCOR_YEASTSPE1genetic
21623372
CBS_YEASTCYS4genetic
21623372
POS5_YEASTPOS5genetic
21623372
TPS1_YEASTTPS1genetic
21623372
PHSG_YEASTGPH1genetic
21623372
HTD2_YEASTHTD2genetic
21623372
FABG_YEASTOAR1genetic
21623372
UGA4_YEASTUGA4genetic
21623372
AMPD_YEASTAMD1physical
22615397
KPYK1_YEASTCDC19genetic
22902555
HOS3_YEASTHOS3genetic
27708008
ETR1_YEASTETR1genetic
27708008
TPS1_YEASTTPS1genetic
27708008
RV161_YEASTRVS161genetic
27708008
RIM1_YEASTRIM1genetic
27708008
IPT1_YEASTIPT1genetic
27708008
CEM1_YEASTCEM1genetic
27708008
RAD4_YEASTRAD4genetic
27708008
DLDH_YEASTLPD1genetic
27708008
SGF73_YEASTSGF73genetic
27708008
HUL5_YEASTHUL5genetic
27708008
HTD2_YEASTHTD2genetic
27708008
LPLA_YEASTAIM22genetic
27708008
YJH0_YEASTYJL070Cgenetic
27708008
BUD2_YEASTBUD2genetic
27708008
UTH1_YEASTUTH1genetic
27708008
RIC1_YEASTRIC1genetic
27708008
MDL1_YEASTMDL1genetic
27708008
TOP3_YEASTTOP3genetic
27708008
MMS22_YEASTMMS22genetic
27708008
VRP1_YEASTVRP1genetic
27708008
ADE_YEASTAAH1genetic
27708008
LIPA_YEASTLIP5genetic
27708008
AFT2_YEASTAFT2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AMPD_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-19; SER-26; SER-58;SER-61; SER-138 AND SER-140, AND MASS SPECTROMETRY.
"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 SER-58; SER-61; THR-136 ANDSER-138, 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-138, AND MASSSPECTROMETRY.
"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-58; SER-61 AND SER-138,AND MASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND MASSSPECTROMETRY.

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