LEUC_YEAST - dbPTM
LEUC_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LEUC_YEAST
UniProt AC P07264
Protein Name 3-isopropylmalate dehydratase
Gene Name LEU1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 779
Subcellular Localization
Protein Description Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate..
Protein Sequence MVYTPSKGPRTLYDKVFDAHVVHQDENGSFLLYIDRHLVHEVTSPQAFEGLENAGRKVRRVDCTLATVDHNIPTESRKNFKSLDTFIKQTDSRLQVKTLENNVKQFGVPYFGMSDARQGIVHTIGPEEGFTLPGTTVVCGDSHTSTHGAFGSLAFGIGTSEVEHVLATQTIIQAKSKNMRITVNGKLSPGITSKDLILYIIGLIGTAGGTGCVIEFAGEAIEALSMEARMSMCNMAIEAGARAGMIKPDETTFQYTKGRPLAPKGAEWEKAVAYWKTLKTDEGAKFDHEINIEAVDVIPTITWGTSPQDALPITGSVPDPKNVTDPIKKSGMERALAYMGLEPNTPLKSIKVDKVFIGSCTNGRIEDLRSAAAVVRGQKLASNIKLAMVVPGSGLVKKQAEAEGLDKIFQEAGFEWREAGCSICLGMNPDILDAYERCASTSNRNFEGRQGALSRTHLMSPAMAAAAGIAGHFVDIREFEYKDQDQSSPKVEVTSEDEKELESAAYDHAEPVQPEDAPQDIANDELKDIPVKSDDTPAKPSSSGMKPFLTLEGISAPLDKANVDTDAIIPKQFLKTIKRTGLKKGLFYEWRFRKDDQGKDQETDFVLNVEPWREAEILVVTGDNFGCGSSREHAPWALKDFGIKSIIAPSYGDIFYNNSFKNGLLPIRLDQQIIIDKLIPIANKGGKLCVDLPNQKILDSDGNVLVDHFEIEPFRKHCLVNGLDDIGITLQKEEYISRYEALRREKYSFLEGGSKLLKFDNVPKRKAVTTTFDKVHQDW
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
4Phosphorylation----MVYTPSKGPRT
----CCCCCCCCCCC		15.0728889911
43PhosphorylationRHLVHEVTSPQAFEG
HHHEEEECCHHHHHH		31.5328132839
44PhosphorylationHLVHEVTSPQAFEGL
HHEEEECCHHHHHHH		21.8617330950
57UbiquitinationGLENAGRKVRRVDCT
HHHHCCCCEEEEECE		38.8915699485
81AcetylationTESRKNFKSLDTFIK
HHHHHHHHHHHHHHH		60.5524489116
81SuccinylationTESRKNFKSLDTFIK
HHHHHHHHHHHHHHH		60.5523954790
81UbiquitinationTESRKNFKSLDTFIK
HHHHHHHHHHHHHHH		60.5524961812
82PhosphorylationESRKNFKSLDTFIKQ
HHHHHHHHHHHHHHH		27.6017563356
85PhosphorylationKNFKSLDTFIKQTDS
HHHHHHHHHHHHCCC		32.3327017623
88AcetylationKSLDTFIKQTDSRLQ
HHHHHHHHHCCCCCE		42.8424489116
97AcetylationTDSRLQVKTLENNVK
CCCCCEEEHHHHHHH		34.1424489116
104AcetylationKTLENNVKQFGVPYF
EHHHHHHHHHCCCCC		41.8724489116
114PhosphorylationGVPYFGMSDARQGIV
CCCCCCCCCCCCCEE		28.6227017623
186AcetylationMRITVNGKLSPGITS
CEEEECCEECCCCCH		40.3624489116
186SuccinylationMRITVNGKLSPGITS
CEEEECCEECCCCCH		40.3623954790
231PhosphorylationLSMEARMSMCNMAIE
HCHHHHHHHHHHHHH		18.0327017623
247UbiquitinationGARAGMIKPDETTFQ
HHHCCCCCCCCCCEE		37.2115699485
247AcetylationGARAGMIKPDETTFQ
HHHCCCCCCCCCCEE		37.2124489116
257UbiquitinationETTFQYTKGRPLAPK
CCCEEEECCCCCCCC		48.2515699485
270AcetylationPKGAEWEKAVAYWKT
CCCCHHHHHHHHHEE		49.5924489116
276AcetylationEKAVAYWKTLKTDEG
HHHHHHHEECCCCCC		31.1624489116
2762-HydroxyisobutyrylationEKAVAYWKTLKTDEG
HHHHHHHEECCCCCC		31.16-
324PhosphorylationVPDPKNVTDPIKKSG
CCCCCCCCCHHHHCC		45.5128889911
328SuccinylationKNVTDPIKKSGMERA
CCCCCHHHHCCHHHH		46.4023954790
330PhosphorylationVTDPIKKSGMERALA
CCCHHHHCCHHHHHH		38.0721440633
345PhosphorylationYMGLEPNTPLKSIKV
HCCCCCCCCCCCCEE		40.4928152593
348AcetylationLEPNTPLKSIKVDKV
CCCCCCCCCCEECEE		51.8724489116
354AcetylationLKSIKVDKVFIGSCT
CCCCEECEEEEECCC		41.8724489116
359PhosphorylationVDKVFIGSCTNGRIE
ECEEEEECCCCCCHH		16.9827017623
361PhosphorylationKVFIGSCTNGRIEDL
EEEEECCCCCCHHHH		42.2628889911
397SuccinylationVPGSGLVKKQAEAEG
ECCCCHHHHHHHHCC		44.1823954790
481PhosphorylationVDIREFEYKDQDQSS
EEEEEEEECCCCCCC		25.7822369663
482AcetylationDIREFEYKDQDQSSP
EEEEEEECCCCCCCC		41.5422865919
487PhosphorylationEYKDQDQSSPKVEVT
EECCCCCCCCCEEEC		57.8222369663
488PhosphorylationYKDQDQSSPKVEVTS
ECCCCCCCCCEEECC		24.0922369663
494PhosphorylationSSPKVEVTSEDEKEL
CCCCEEECCCCHHHH		16.9425521595
495PhosphorylationSPKVEVTSEDEKELE
CCCEEECCCCHHHHH		48.5022369663
503PhosphorylationEDEKELESAAYDHAE
CCHHHHHHHHCCCCC		30.7222369663
506PhosphorylationKELESAAYDHAEPVQ
HHHHHHHCCCCCCCC		14.1522369663
533PhosphorylationLKDIPVKSDDTPAKP
HCCCCCCCCCCCCCC		40.7422369663
536PhosphorylationIPVKSDDTPAKPSSS
CCCCCCCCCCCCCCC		30.0922369663
539AcetylationKSDDTPAKPSSSGMK
CCCCCCCCCCCCCCC		46.7824489116
541PhosphorylationDDTPAKPSSSGMKPF
CCCCCCCCCCCCCCE		36.1122369663
542PhosphorylationDTPAKPSSSGMKPFL
CCCCCCCCCCCCCEE		39.1622369663
543PhosphorylationTPAKPSSSGMKPFLT
CCCCCCCCCCCCEEE		47.4422369663
546AcetylationKPSSSGMKPFLTLEG
CCCCCCCCCEEEEEC		35.8224489116
550PhosphorylationSGMKPFLTLEGISAP
CCCCCEEEEECCCCC		24.1222369663
555PhosphorylationFLTLEGISAPLDKAN
EEEEECCCCCHHHCC		34.3922369663
571AcetylationDTDAIIPKQFLKTIK
CCCCCCCHHHHHHHH		43.1824489116
584AcetylationIKRTGLKKGLFYEWR
HHHHCCCCCCEEEEE		66.9322865919
599AcetylationFRKDDQGKDQETDFV
EEECCCCCCCCCCEE		51.0824489116
639AcetylationEHAPWALKDFGIKSI
CCCCCHHHHHCCCCE		43.1724489116
644UbiquitinationALKDFGIKSIIAPSY
HHHHHCCCCEECCCC		35.6624961812
661UbiquitinationIFYNNSFKNGLLPIR
CCCCCCCCCCCCCCE		50.3415699485
677AcetylationDQQIIIDKLIPIANK
CCEEHHHHHHHCCCC		37.6024489116
687AcetylationPIANKGGKLCVDLPN
HCCCCCCCEEEECCC		47.5924489116
696AcetylationCVDLPNQKILDSDGN
EEECCCCEEECCCCC		52.4525381059
737PhosphorylationLQKEEYISRYEALRR
ECHHHHHHHHHHHHH		28.1024961812
739PhosphorylationKEEYISRYEALRREK
HHHHHHHHHHHHHHC		9.9624961812
746AcetylationYEALRREKYSFLEGG
HHHHHHHCCCCHHCC		44.3724489116
747PhosphorylationEALRREKYSFLEGGS
HHHHHHCCCCHHCCC		10.4124961812
748PhosphorylationALRREKYSFLEGGSK
HHHHHCCCCHHCCCC		34.1321551504
754PhosphorylationYSFLEGGSKLLKFDN
CCCHHCCCCEECCCC		30.8724961812
755UbiquitinationSFLEGGSKLLKFDNV
CCHHCCCCEECCCCC		62.2024961812
755AcetylationSFLEGGSKLLKFDNV
CCHHCCCCEECCCCC		62.2024489116
758AcetylationEGGSKLLKFDNVPKR
HCCCCEECCCCCCCC		62.1924489116
764AcetylationLKFDNVPKRKAVTTT
ECCCCCCCCCEEECC		63.3525381059
769PhosphorylationVPKRKAVTTTFDKVH
CCCCCEEECCHHHHC		25.6128889911
770PhosphorylationPKRKAVTTTFDKVHQ
CCCCEEECCHHHHCC		20.9027717283
771PhosphorylationKRKAVTTTFDKVHQD
CCCEEECCHHHHCCC		22.0728889911
774AcetylationAVTTTFDKVHQDW--
EEECCHHHHCCCC--		37.1124489116
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 LEUC_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LEUC_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 LEUC_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ADH1_YEASTADH1physical
11805826
SYMM_YEASTMSM1physical
16554755
RTG2_YEASTRTG2genetic
20093466
LRP1_YEASTLRP1genetic
20093466
YJB6_YEASTYJL016Wgenetic
20093466
RL22A_YEASTRPL22Agenetic
20093466
UPS1_YEASTUPS1genetic
20093466
ELO3_YEASTELO3genetic
20093466
MKS1_YEASTMKS1genetic
20093466
MED9_YEASTCSE2genetic
20093466
LGE1_YEASTLGE1genetic
20093466
THP3_YEASTTHP3genetic
20093466
FCY2_YEASTFCY2genetic
21623372
ADH1_YEASTADH1genetic
21623372
IDH2_YEASTIDH2genetic
21623372
HFA1_YEASTHFA1genetic
21623372
COX8_YEASTCOX8genetic
21623372
PFKA1_YEASTPFK1genetic
21623372
COX6_YEASTCOX6genetic
21623372
ATPA_YEASTATP1genetic
21623372
ELO2_YEASTELO2genetic
21623372
SDHA_YEASTSDH1genetic
21623372
DAL4_YEASTDAL4genetic
21623372
COX9_YEASTCOX9genetic
21623372
COX5A_YEASTCOX5Agenetic
21623372
DHAS_YEASTHOM2genetic
21623372
GGPPS_YEASTBTS1genetic
21623372
TRXB2_YEASTTRR2genetic
21623372
ODO2_YEASTKGD2genetic
21623372
ACON_YEASTACO1genetic
21623372
COQ7_YEASTCAT5genetic
21623372
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LEUC_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-4; THR-361; SER-487;SER-488; THR-494; SER-495 AND SER-748, 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-82; SER-488; SER-495;SER-503; THR-536 AND SER-748, 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-488 AND SER-495, ANDMASS SPECTROMETRY.
"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-488, 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-494, AND MASSSPECTROMETRY.

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