MET3_YEAST - dbPTM
MET3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MET3_YEAST
UniProt AC P08536
Protein Name Sulfate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_03106}
Gene Name MET3 {ECO:0000255|HAMAP-Rule:MF_03106}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 511
Subcellular Localization Cytoplasm .
Protein Description Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids..
Protein Sequence MPAPHGGILQDLIARDALKKNELLSEAQSSDILVWNLTPRQLCDIELILNGGFSPLTGFLNENDYSSVVTDSRLADGTLWTIPITLDVDEAFANQIKPDTRIALFQDDEIPIAILTVQDVYKPNKTIEAEKVFRGDPEHPAISYLFNVAGDYYVGGSLEAIQLPQHYDYPGLRKTPAQLRLEFQSRQWDRVVAFQTRNPMHRAHRELTVRAAREANAKVLIHPVVGLTKPGDIDHHTRVRVYQEIIKRYPNGIAFLSLLPLAMRMSGDREAVWHAIIRKNYGASHFIVGRDHAGPGKNSKGVDFYGPYDAQELVESYKHELDIEVVPFRMVTYLPDEDRYAPIDQIDTTKTRTLNISGTELRRRLRVGGEIPEWFSYPEVVKILRESNPPRPKQGFSIVLGNSLTVSREQLSIALLSTFLQFGGGRYYKIFEHNNKTELLSLIQDFIGSGSGLIIPNQWEDDKDSVVGKQNVYLLDTSSSADIQLESADEPISHIVQKVVLFLEDNGFFVF
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
126PhosphorylationDVYKPNKTIEAEKVF
CCCCCCCEEEEEEEC
30.5915665377
357PhosphorylationKTRTLNISGTELRRR
CCEEEECCHHHHHHH
38.2928889911
359PhosphorylationRTLNISGTELRRRLR
EEEECCHHHHHHHHC
25.6728152593

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 MET3_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MET3_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 MET3_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MET3_YEASTMET3physical
11283351
MET3_YEASTMET3physical
14983089
THDH_YEASTILV1genetic
21623372
FOLE_YEASTMET7genetic
21623372
ARGJ_YEASTARG7genetic
21623372
MET3_YEASTMET3physical
22615397
TRS20_YEASTTRS20genetic
27708008
APC11_YEASTAPC11genetic
27708008
SNU23_YEASTSNU23genetic
27708008
UAP1_YEASTQRI1genetic
27708008
RPB1_YEASTRPO21genetic
27708008
CDC1_YEASTCDC1genetic
27708008
TRS23_YEASTTRS23genetic
27708008
ACT_YEASTACT1genetic
27708008
CDC20_YEASTCDC20genetic
27708008
DBF2_YEASTDBF2genetic
27708008
PRP21_YEASTPRP21genetic
27708008
UGPA1_YEASTUGP1genetic
27708008
PRS7_YEASTRPT1genetic
27708008
BOS1_YEASTBOS1genetic
27708008
AFG2_YEASTAFG2genetic
27708008
VTI1_YEASTVTI1genetic
27708008
DCP2_YEASTDCP2genetic
27708008
PRP2_YEASTPRP2genetic
27708008
RPB2_YEASTRPB2genetic
27708008
GRPE_YEASTMGE1genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MET3_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-359, AND MASSSPECTROMETRY.
"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 THR-126, AND MASSSPECTROMETRY.

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