LYS2_YEAST - dbPTM
LYS2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LYS2_YEAST
UniProt AC P07702
Protein Name L-2-aminoadipate reductase
Gene Name LYS2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1392
Subcellular Localization
Protein Description Catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate..
Protein Sequence MTNEKVWIEKLDNPTLSVLPHDFLRPQQEPYTKQATYSLQLPQLDVPHDSFSNKYAVALSVWAALIYRVTGDDDIVLYIANNKILRFNIQPTWSFNELYSTINNELNKLNSIEANFSFDELAEKIQSCQDLERTPQLFRLAFLENQDFKLDEFKHHLVDFALNLDTSNNAHVLNLIYNSLLYSNERVTIVADQFTQYLTAALSDPSNCITKISLITASSKDSLPDPTKNLGWCDFVGCIHDIFQDNAEAFPERTCVVETPTLNSDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRGLIVIRAAGQLDQLVEDYINDELEIVSRINSIAIQENGTIEGGKLDNGEDVLAPYDHYKDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDIGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETQRAVSYFEVKSKNDDPNFLKKLKDVMPAGKGMLNVQLLVVNRNDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEKDHWNYLDKDNGEPWRQFWLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRKNADNEPTLITFMVPRFDKPDDLSKFQSDVPKEVETDPIVKGLIGYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKLQFPTPKQLNLVAENTVSETDDSQFTNVEREVRDLWLSILPTKPASVSPDDSFFDLGGHSILATKMIFTLKKKLQVDLPLGTIFKYPTIKAFAAEIDRIKSSGGSSQGEVVENVTANYAEDAKKLVETLPSSYPSREYFVEPNSAEGKTTINVFVTGVTGFLGSYILADLLGRSPKNYSFKVFAHVRAKDEEAAFARLQKAGITYGTWNEKFASNIKVVLGDLSKSQFGLSDEKWMDLANTVDIIIHNGALVHWVYPYAKLRDPNVISTINVMSLAAVGKPKFFDFVSSTSTLDTEYYFNLSDKLVSEGKPGILESDDLMNSASGLTGGYGQSKWAAEYIIRRAGERGLRGCIVRPGYVTGASANGSSNTDDFLLRFLKGSVQLGKIPDIENSVNMVPVDHVARVVVATSLNPPKENELAVAQVTGHPRILFKDYLYTLHDYGYDVEIESYSKWKKSLEASVIDRNEENALYPLLHMVLDNLPESTKAPELDDRNAVASLKKDTAWTGVDWSNGIGVTPEEVGIYIAFLNKVGFLPPPTHNDKLPLPSIELTQAQISLVASGAGARGSSAAA
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
5Ubiquitination---MTNEKVWIEKLD
---CCCCCEEEEECC		44.9617644757
10UbiquitinationNEKVWIEKLDNPTLS
CCCEEEEECCCCCCC		52.5917644757
33UbiquitinationPQQEPYTKQATYSLQ
CCCCCCCCCCEEEEE		31.9017644757
211UbiquitinationDPSNCITKISLITAS
CCCCCEEEEEEEEEC		15.4715699485
213PhosphorylationSNCITKISLITASSK
CCCEEEEEEEEECCC		18.4421126336
216PhosphorylationITKISLITASSKDSL
EEEEEEEEECCCCCC		26.2721126336
220UbiquitinationSLITASSKDSLPDPT
EEEEECCCCCCCCCC		49.1715699485
228UbiquitinationDSLPDPTKNLGWCDF
CCCCCCCCCCCCCCH		56.4117644757
288UbiquitinationIVAHYLIKTGIKRGD
HHHHHHHHCCCCCCC		37.8017644757
301PhosphorylationGDVVMIYSSRGVDLM
CCEEEEEECCCCCEE		11.5727017623
328PhosphorylationFSVIDPAYPPARQTI
EEECCCCCCCHHCEE		18.3527017623
334PhosphorylationAYPPARQTIYLGVAK
CCCCHHCEEEEEECC		13.1627017623
336PhosphorylationPPARQTIYLGVAKPR
CCHHCEEEEEECCCC		10.7827017623
429UbiquitinationSGSEGIPKGVLGRHF
CCCCCCCCCCCCCHH		60.7817644757
528UbiquitinationQATTPFPKLHHAFFV
CCCCCCCCCCEEEHH		61.9117644757
541UbiquitinationFVGDILTKRDCLRLQ
HHHHHCCHHHHHHHH		42.6722106047
703AcetylationGRADDQVKIRGFRIE
CCCCCCEEECEEEEE		22.5125381059
880PhosphorylationFFDLGGHSILATKMI
CCCCCCCHHHHHHHH		23.6710320345
880O-(pantetheine 4'-phosphoryl)serineFFDLGGHSILATKMI
CCCCCCCHHHHHHHH		23.67-
905AcetylationLPLGTIFKYPTIKAF
CCCCHHCCCHHHHHH		46.6125381059
925PhosphorylationRIKSSGGSSQGEVVE
HHHCCCCCCHHEEEE		24.0227214570
926PhosphorylationIKSSGGSSQGEVVEN
HHCCCCCCHHEEEEE		45.5427214570
1009AcetylationVFAHVRAKDEEAAFA
EEEEEEECCHHHHHH		55.9225381059
1130UbiquitinationDKLVSEGKPGILESD
HHHHHCCCCCCCCCH		35.7022106047
1235UbiquitinationATSLNPPKENELAVA
EECCCCCCCCCCEEE		74.5517644757
1276UbiquitinationESYSKWKKSLEASVI
EEHHHHHHHHHEEEE		60.1922106047
1363UbiquitinationPPPTHNDKLPLPSIE
CCCCCCCCCCCCCEE		58.2717644757
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 LYS2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LYS2_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 LYS2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LYS5_YEASTLYS5physical
11805826
SPT2_YEASTSPT2genetic
6326126
SPT3_YEASTSPT3genetic
6326126
H4_YEASTHHF1genetic
9171362
LYS5_YEASTLYS5physical
16429126
RS4A_YEASTRPS4Aphysical
16429126
RS4B_YEASTRPS4Aphysical
16429126
HSP71_YEASTSSA1physical
19536198
RRP6_YEASTRRP6genetic
16832048
NCBP1_YEASTSTO1genetic
16832048
NAM7_YEASTNAM7genetic
16832048
ECM21_YEASTECM21genetic
23091010
UBP4_YEASTDOA4genetic
23091010
RSP5_YEASTRSP5genetic
23091010
BRO1_YEASTBRO1genetic
23091010
LYP1_YEASTLYP1genetic
23091010
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LYS2_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-926, AND MASSSPECTROMETRY.

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