APA1_YEAST - dbPTM
APA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APA1_YEAST
UniProt AC P16550
Protein Name Protein APA1
Gene Name APA1 {ECO:0000303|PubMed:2556364}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 321
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Ap4A phosphorylase catalyzes the phosphorolytic degradation of bis(5'-adenosyl) tetraphosphate (Ap4A) into ADP and ATP. Can also use other Np4N' nucleotides (where N and N' stand for A,C,G or U) as substrates with equal efficiency. Cannot catalyze the reverse reaction. Additionally, this enzyme can also catalyze the phosphorolytic degradation of adenosine 5'-phosphosulfate (AMPS) into ADP and sulfate, the reversible exchange reaction between inorganic phosphate and the beta-phosphate of a nucleoside diphosphate (NDP), and the synthesis of Ap4A from AMPS plus ATP..
Protein Sequence MSIPADIASLISDKYKSAFDNGNLKFIQTETTKTKDPKTSMPYLISHMPSLIEKPERGQTPEGEDPLGKPEEELTVIPEFGGADNKAYKLLLNKFPVIPEHTLLVTNEYQHQTDALTPTDLLTAYKLLCALDNEESDKRHMVFYNSGPASGSSLDHKHLQILQMPEKFVTFQDRLCNGKEHFLPTFNTEPLQDAKVSFAHFVLPMPESEETVDEDLLAMCYISILQRALTFFQDWLNENPELKKSYNLMLTKEWICVVPRSKAFSDEMKIGFNSTGYCGMILTKNDEVFSKITEKPELINDILLECGFPNTSGQKPNEYNY
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------MSIPADIAS
------CCCCHHHHH		36.9619823750
9PhosphorylationSIPADIASLISDKYK
CCCHHHHHHHCHHHH		26.9428152593
12PhosphorylationADIASLISDKYKSAF
HHHHHHHCHHHHHHH		33.0919823750
17PhosphorylationLISDKYKSAFDNGNL
HHCHHHHHHHHCCCE		30.9528889911
25AcetylationAFDNGNLKFIQTETT
HHHCCCEEEEEEEEC		44.4124489116
43PhosphorylationDPKTSMPYLISHMPS
CCCCCHHHHHHCCHH		14.1828889911
46PhosphorylationTSMPYLISHMPSLIE
CCHHHHHHCCHHHHC		15.9028889911
50PhosphorylationYLISHMPSLIEKPER
HHHHCCHHHHCCCCC		34.1128889911
54AcetylationHMPSLIEKPERGQTP
CCHHHHCCCCCCCCC		45.2224489116
60PhosphorylationEKPERGQTPEGEDPL
CCCCCCCCCCCCCCC		26.5722369663
69AcetylationEGEDPLGKPEEELTV
CCCCCCCCCHHHEEE		57.8724489116
75PhosphorylationGKPEEELTVIPEFGG
CCCHHHEEECCCCCC		21.4822890988
86AcetylationEFGGADNKAYKLLLN
CCCCCCHHHHHHHHH		54.3524489116
126UbiquitinationTDLLTAYKLLCALDN
HHHHHHHHHHHHCCC		32.3015699485
138AcetylationLDNEESDKRHMVFYN
CCCCCCCCCEEEEEE		54.1824489116
138UbiquitinationLDNEESDKRHMVFYN
CCCCCCCCCEEEEEE		54.1823749301
157AcetylationSGSSLDHKHLQILQM
CCCCCCHHHHHHHCC		45.7524489116
167UbiquitinationQILQMPEKFVTFQDR
HHHCCCCCEEEHHHH		38.9823749301
167AcetylationQILQMPEKFVTFQDR
HHHCCCCCEEEHHHH		38.9824489116
179AcetylationQDRLCNGKEHFLPTF
HHHHHCCCCCCCCCC		33.7424489116
185PhosphorylationGKEHFLPTFNTEPLQ
CCCCCCCCCCCCCCC		31.5017563356
284AcetylationYCGMILTKNDEVFSK
CCEEEEECCHHHHHH		59.9824489116
284UbiquitinationYCGMILTKNDEVFSK
CCEEEEECCHHHHHH		59.9823749301
291UbiquitinationKNDEVFSKITEKPEL
CCHHHHHHHCCCHHH		42.0315699485
295UbiquitinationVFSKITEKPELINDI
HHHHHCCCHHHHHHH		34.8315699485
315UbiquitinationFPNTSGQKPNEYNY-
CCCCCCCCCCCCCC-		54.0215699485
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 APA1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of APA1_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 APA1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MET3_YEASTMET3genetic
16941010
SDS24_YEASTSDS24genetic
27708008
UME6_YEASTUME6genetic
27708008
RLA4_YEASTRPP2Bgenetic
27708008
CGR1_YEASTCGR1genetic
27708008
LRP1_YEASTLRP1genetic
27708008
YIA6_YEASTYIA6genetic
27708008
ILM1_YEASTILM1genetic
27708008
ALAM_YEASTALT1genetic
27708008
ERG2_YEASTERG2genetic
27708008
RCF2_YEASTRCF2genetic
27708008
WDR6_YEASTRTT10genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of APA1_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 THR-60, AND MASSSPECTROMETRY.
"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 THR-60 AND THR-185, 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 THR-60, AND MASSSPECTROMETRY.

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