SAHH_YEAST - dbPTM
SAHH_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAHH_YEAST
UniProt AC P39954
Protein Name Adenosylhomocysteinase
Gene Name SAH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 449
Subcellular Localization
Protein Description Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine..
Protein Sequence MSAPAQNYKIADISLAAFGRKEIELAEHEMPGLMAIRKAYGDVQPLKGARIAGCLHMTIQTAVLIETLVALGAEVTWSSCNIYSTQDHAAAAIAASGVPVFAWKGETEEEYLWCIEQQLFAFKDNKKLNLILDDGGDLTTLVHEKHPEMLEDCFGLSEETTTGVHHLYRMVKEGKLKVPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMLAGKVAVVAGYGDVGKGCAAALRGMGARVLVTEIDPINALQAAMEGYQVVTMEDASHIGQVFVTTTGCRDIINGEHFINMPEDAIVCNIGHFDIEIDVAWLKANAKECINIKPQVDRYLLSSGRHVILLANGRLVNLGCATGHSSFVMSCSFSNQVLAQIALFKSNDKSFREKHIEFQKTGPFEVGVHVLPKILDEAVAKFHLGNLGVRLTKLSKVQSEYLGIPEEGPFKADHYRY
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------MSAPAQNYK
------CCCCCCCCC		42.8522369663
2Acetylation------MSAPAQNYK
------CCCCCCCCC		42.8522814378
8PhosphorylationMSAPAQNYKIADISL
CCCCCCCCCEEEEEH		7.5319823750
9SuccinylationSAPAQNYKIADISLA
CCCCCCCCEEEEEHH		38.6823954790
9AcetylationSAPAQNYKIADISLA
CCCCCCCCEEEEEHH		38.6824489116
9UbiquitinationSAPAQNYKIADISLA
CCCCCCCCEEEEEHH		38.6824961812
14PhosphorylationNYKIADISLAAFGRK
CCCEEEEEHHHHCCC		16.7121440633
21UbiquitinationSLAAFGRKEIELAEH
EHHHHCCCHHHHHHC		64.5223749301
38UbiquitinationPGLMAIRKAYGDVQP
CCHHHHHHHHCCCCC		39.5923749301
38SuccinylationPGLMAIRKAYGDVQP
CCHHHHHHHHCCCCC		39.5923954790
38AcetylationPGLMAIRKAYGDVQP
CCHHHHHHHHCCCCC		39.5922865919
47UbiquitinationYGDVQPLKGARIAGC
HCCCCCCCCCCHHHH		58.1523749301
47AcetylationYGDVQPLKGARIAGC
HCCCCCCCCCCHHHH		58.1524489116
47SuccinylationYGDVQPLKGARIAGC
HCCCCCCCCCCHHHH		58.1523954790
472-HydroxyisobutyrylationYGDVQPLKGARIAGC
HCCCCCCCCCCHHHH		58.15-
127AcetylationFAFKDNKKLNLILDD
EECCCCCEEEEEEEC		49.1917397211
177UbiquitinationMVKEGKLKVPAINVN
HHHCCCCCCCEEECC		50.0523749301
1772-HydroxyisobutyrylationMVKEGKLKVPAINVN
HHHCCCCCCCEEECC		50.05-
186PhosphorylationPAINVNDSVTKSKFD
CEEECCCCCCHHHCC		26.8721440633
188PhosphorylationINVNDSVTKSKFDNL
EECCCCCCHHHCCCC		33.2928889911
1892-HydroxyisobutyrylationNVNDSVTKSKFDNLY
ECCCCCCHHHCCCCC		49.87-
189UbiquitinationNVNDSVTKSKFDNLY
ECCCCCCHHHCCCCC		49.8723749301
189AcetylationNVNDSVTKSKFDNLY
ECCCCCCHHHCCCCC		49.8724489116
191AcetylationNDSVTKSKFDNLYGC
CCCCCHHHCCCCCCH		59.2924489116
191UbiquitinationNDSVTKSKFDNLYGC
CCCCCHHHCCCCCCH		59.2923749301
201PhosphorylationNLYGCRESLVDGIKR
CCCCHHHHHHHHHHH		17.8430377154
207AcetylationESLVDGIKRATDVML
HHHHHHHHHHHHHHH		41.3222865919
207UbiquitinationESLVDGIKRATDVML
HHHHHHHHHHHHHHH		41.3223749301
207SuccinylationESLVDGIKRATDVML
HHHHHHHHHHHHHHH		41.3223954790
229UbiquitinationAGYGDVGKGCAAALR
ECCCCHHHHHHHHHH		51.1423749301
315UbiquitinationEIDVAWLKANAKECI
EEEHHHHHCCHHHHH		28.9722817900
319UbiquitinationAWLKANAKECINIKP
HHHHCCHHHHHCCCH		53.5823749301
319AcetylationAWLKANAKECINIKP
HHHHCCHHHHHCCCH		53.5824489116
319SuccinylationAWLKANAKECINIKP
HHHHCCHHHHHCCCH		53.5823954790
325UbiquitinationAKECINIKPQVDRYL
HHHHHCCCHHHHHHH		25.5523749301
325AcetylationAKECINIKPQVDRYL
HHHHHCCCHHHHHHH		25.5524489116
325SuccinylationAKECINIKPQVDRYL
HHHHHCCCHHHHHHH		25.5523954790
334PhosphorylationQVDRYLLSSGRHVIL
HHHHHHHCCCCEEEE		28.3122369663
335PhosphorylationVDRYLLSSGRHVILL
HHHHHHCCCCEEEEE		39.5522369663
381SuccinylationALFKSNDKSFREKHI
HHHHCCCHHHHHHHE		56.6023954790
381AcetylationALFKSNDKSFREKHI
HHHHCCCHHHHHHHE		56.6024489116
386AcetylationNDKSFREKHIEFQKT
CCHHHHHHHEEEECC		45.7024489116
392AcetylationEKHIEFQKTGPFEVG
HHHEEEECCCCCCCE		61.8524489116
393PhosphorylationKHIEFQKTGPFEVGV
HHEEEECCCCCCCEE		39.0322369663
405AcetylationVGVHVLPKILDEAVA
CEEEEHHHHHHHHHH		52.3024489116
405UbiquitinationVGVHVLPKILDEAVA
CEEEEHHHHHHHHHH		52.3024961812
413AcetylationILDEAVAKFHLGNLG
HHHHHHHHHHHCCHH		27.0724489116
413UbiquitinationILDEAVAKFHLGNLG
HHHHHHHHHHHCCHH		27.0723749301
424PhosphorylationGNLGVRLTKLSKVQS
CCHHHHHHHHHHHCH		21.2624961812
427PhosphorylationGVRLTKLSKVQSEYL
HHHHHHHHHHCHHHC		32.1324961812
428UbiquitinationVRLTKLSKVQSEYLG
HHHHHHHHHCHHHCC		55.5223749301
428AcetylationVRLTKLSKVQSEYLG
HHHHHHHHHCHHHCC		55.5224489116
431PhosphorylationTKLSKVQSEYLGIPE
HHHHHHCHHHCCCCC		31.0625752575
443AcetylationIPEEGPFKADHYRY-
CCCCCCCCCCCCCC-		56.9124489116
443UbiquitinationIPEEGPFKADHYRY-
CCCCCCCCCCCCCC-		56.9124961812
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 SAHH_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAHH_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 SAHH_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CYSD_YEASTMET17genetic
18591246
ERC1_YEASTERC1genetic
27698120
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SAHH_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-393, AND MASSSPECTROMETRY.
"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-393, 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-393, AND MASSSPECTROMETRY.

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