HOSC_YEAST - dbPTM
HOSC_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HOSC_YEAST
UniProt AC P48570
Protein Name Homocitrate synthase, cytosolic isozyme
Gene Name LYS20
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 428
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MTAAKPNPYAAKPGDYLSNVNNFQLIDSTLREGEQFANAFFDTEKKIEIARALDDFGVDYIELTSPVASEQSRKDCEAICKLGLKAKILTHIRCHMDDAKVAVETGVDGVDVVIGTSKFLRQYSHGKDMNYIAKSAVEVIEFVKSKGIEIRFSSEDSFRSDLVDLLNIYKTVDKIGVNRVGIADTVGCANPRQVYELIRTLKSVVSCDIECHFHNDTGCAIANAYTALEGGARLIDVSVLGIGERNGITPLGGLMARMIVAAPDYVKSKYKLHKIRDIENLVADAVEVNIPFNNPITGFCAFTHKAGIHAKAILANPSTYEILDPHDFGMKRYIHFANRLTGWNAIKARVDQLNLNLTDDQIKEVTAKIKKLGDVRSLNIDDVDSIIKNFHAEVSTPQVLSAKKNKKNDSDVPELATIPAAKRTKPSA
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------MTAAKPNPY
------CCCCCCCCC		35.0122369663
9PhosphorylationTAAKPNPYAAKPGDY
CCCCCCCCCCCCCCC		26.3222369663
45UbiquitinationNAFFDTEKKIEIARA
HHHCCHHHHHHHHHH		62.2317644757
45AcetylationNAFFDTEKKIEIARA
HHHCCHHHHHHHHHH		62.2324489116
46UbiquitinationAFFDTEKKIEIARAL
HHCCHHHHHHHHHHH		39.0617644757
60PhosphorylationLDDFGVDYIELTSPV
HHHHCCCEEEECCCC		8.2222369663
64PhosphorylationGVDYIELTSPVASEQ
CCCEEEECCCCCCHH		20.4222369663
65PhosphorylationVDYIELTSPVASEQS
CCEEEECCCCCCHHH		29.9622369663
69PhosphorylationELTSPVASEQSRKDC
EECCCCCCHHHHHHH		36.0822369663
72PhosphorylationSPVASEQSRKDCEAI
CCCCCHHHHHHHHHH		36.9322369663
74UbiquitinationVASEQSRKDCEAICK
CCCHHHHHHHHHHHH		72.4817644757
74AcetylationVASEQSRKDCEAICK
CCCHHHHHHHHHHHH		72.4825381059
81AcetylationKDCEAICKLGLKAKI
HHHHHHHHHHHHHHH		39.2024489116
118AcetylationDVVIGTSKFLRQYSH
EEEEECHHHHHHHHC		48.5325381059
127AcetylationLRQYSHGKDMNYIAK
HHHHHCCCCHHHHHH		48.6724489116
134UbiquitinationKDMNYIAKSAVEVIE
CCHHHHHHHHHHHHH		29.4117644757
134AcetylationKDMNYIAKSAVEVIE
CCHHHHHHHHHHHHH		29.4124489116
144UbiquitinationVEVIEFVKSKGIEIR
HHHHHHHHHCCCEEE		52.3417644757
144AcetylationVEVIEFVKSKGIEIR
HHHHHHHHHCCCEEE		52.3424489116
154PhosphorylationGIEIRFSSEDSFRSD
CCEEEECCCCCCCHH		42.5930377154
170UbiquitinationVDLLNIYKTVDKIGV
HHHHHHHHHHHHCCC		37.9724961812
170AcetylationVDLLNIYKTVDKIGV
HHHHHHHHHHHHCCC		37.9724489116
174AcetylationNIYKTVDKIGVNRVG
HHHHHHHHCCCCCCC		36.7022865919
202UbiquitinationYELIRTLKSVVSCDI
HHHHHHHHHHHCCEE		40.3617644757
203PhosphorylationELIRTLKSVVSCDIE
HHHHHHHHHHCCEEE		30.7528889911
267UbiquitinationVAAPDYVKSKYKLHK
HHCHHHHHHHHHHHC		34.6915699485
267AcetylationVAAPDYVKSKYKLHK
HHCHHHHHHHHHHHC		34.6924489116
274UbiquitinationKSKYKLHKIRDIENL
HHHHHHHCHHCHHHH		50.2817644757
305UbiquitinationGFCAFTHKAGIHAKA
CEEEECCCCCCCCEE		45.2917644757
311UbiquitinationHKAGIHAKAILANPS
CCCCCCCEEEECCCC		23.0724961812
311AcetylationHKAGIHAKAILANPS
CCCCCCCEEEECCCC		23.0724489116
318PhosphorylationKAILANPSTYEILDP
EEEECCCCCCCCCCH		43.3522369663
319PhosphorylationAILANPSTYEILDPH
EEECCCCCCCCCCHH		26.8222369663
320PhosphorylationILANPSTYEILDPHD
EECCCCCCCCCCHHH		12.8122369663
331AcetylationDPHDFGMKRYIHFAN
CHHHHCHHHHHHHHH		42.2924489116
331UbiquitinationDPHDFGMKRYIHFAN
CHHHHCHHHHHHHHH		42.2923749301
347AcetylationLTGWNAIKARVDQLN
HHCHHHHHHHHHHHC		27.9425381059
347UbiquitinationLTGWNAIKARVDQLN
HHCHHHHHHHHHHHC		27.9417644757
363UbiquitinationNLTDDQIKEVTAKIK
CCCHHHHHHHHHHHH		40.2617644757
363AcetylationNLTDDQIKEVTAKIK
CCCHHHHHHHHHHHH		40.2624489116
368UbiquitinationQIKEVTAKIKKLGDV
HHHHHHHHHHHHCCC		45.7717644757
377PhosphorylationKKLGDVRSLNIDDVD
HHHCCCCCCCHHHHH		26.1423749301
385PhosphorylationLNIDDVDSIIKNFHA
CCHHHHHHHHHHHHH		26.5128152593
388UbiquitinationDDVDSIIKNFHAEVS
HHHHHHHHHHHHHCC		52.4717644757
395PhosphorylationKNFHAEVSTPQVLSA
HHHHHHCCCHHHHHC		26.3522369663
396PhosphorylationNFHAEVSTPQVLSAK
HHHHHCCCHHHHHCH		23.9422369663
401PhosphorylationVSTPQVLSAKKNKKN
CCCHHHHHCHHCCCC		38.9022369663
403AcetylationTPQVLSAKKNKKNDS
CHHHHHCHHCCCCCC		54.2025381059
403UbiquitinationTPQVLSAKKNKKNDS
CHHHHHCHHCCCCCC		54.2024961812
404UbiquitinationPQVLSAKKNKKNDSD
HHHHHCHHCCCCCCC		73.9617644757
404AcetylationPQVLSAKKNKKNDSD
HHHHHCHHCCCCCCC		73.9625381059
406UbiquitinationVLSAKKNKKNDSDVP
HHHCHHCCCCCCCCC		62.9317644757
407AcetylationLSAKKNKKNDSDVPE
HHCHHCCCCCCCCCH		75.3225381059
407UbiquitinationLSAKKNKKNDSDVPE
HHCHHCCCCCCCCCH		75.3217644757
410PhosphorylationKKNKKNDSDVPELAT
HHCCCCCCCCCHHHC		50.3122369663
417PhosphorylationSDVPELATIPAAKRT
CCCCHHHCCCHHHCC		39.8722369663
422UbiquitinationLATIPAAKRTKPSA-
HHCCCHHHCCCCCC-		63.8117644757
422AcetylationLATIPAAKRTKPSA-
HHCCCHHHCCCCCC-		63.8124489116
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 HOSC_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HOSC_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 HOSC_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YBI6_YEASTYBL086Cphysical
16554755
RS9B_YEASTRPS9Bphysical
16554755
HOSM_YEASTLYS21physical
16554755
HMO1_YEASTHMO1physical
16554755
YRA1_YEASTYRA1physical
16554755
RL37B_YEASTRPL37Bphysical
16554755
GLO3_YEASTGLO3physical
16554755
PUF4_YEASTPUF4physical
16554755
DPH1_YEASTDPH1physical
16554755
RL43A_YEASTRPL43Bphysical
16554755
RL43B_YEASTRPL43Bphysical
16554755
T2EB_YEASTTFA2physical
16554755
STM1_YEASTSTM1physical
16554755
RRP5_YEASTRRP5physical
16554755
NAT10_YEASTKRE33physical
16554755
ISA2_YEASTISA2physical
16554755
NAP1_YEASTNAP1physical
16554755
RL10_YEASTRPL10physical
16554755
HOSC_YEASTLYS20physical
18467557
HOSM_YEASTLYS21genetic
18408719
KMO_YEASTBNA4genetic
16941010
I23O_YEASTBNA2genetic
16941010
KYNU_YEASTBNA5genetic
16941010
SDH3_YEASTSDH3genetic
16941010
HOSM_YEASTLYS21genetic
18524920
GLYM_YEASTSHM1genetic
20093466
SSH1_YEASTSSH1genetic
20093466
TXTP_YEASTCTP1genetic
20093466
MGR1_YEASTMGR1genetic
20093466
STE50_YEASTSTE50genetic
20093466
THRC_YEASTTHR4genetic
20093466
ATG15_YEASTATG15genetic
20093466
MTU1_YEASTSLM3genetic
20093466
SLX5_YEASTSLX5genetic
20093466
CAJ1_YEASTCAJ1genetic
20093466
GCN20_YEASTGCN20genetic
20093466
SDS3_YEASTSDS3genetic
20093466
ATP18_YEASTATP18genetic
20093466
YHM2_YEASTYHM2genetic
20093466
SCS7_YEASTSCS7genetic
20093466
UBP15_YEASTUBP15genetic
20093466
GAS1_YEASTGAS1genetic
20093466
MKS1_YEASTMKS1genetic
20093466
COX5A_YEASTCOX5Agenetic
20093466
IDH1_YEASTIDH1genetic
20093466
MED9_YEASTCSE2genetic
20093466
HST1_YEASTHST1genetic
20093466
RTG1_YEASTRTG1genetic
20093466
IDH2_YEASTIDH2genetic
20093466
LIPA_YEASTLIP5genetic
20093466
HAP5_YEASTHAP5genetic
20093466
MDL2_YEASTMDL2genetic
20093466
MSS18_YEASTMSS18genetic
20093466
H2AZ_YEASTHTZ1genetic
20810648
ESA1_YEASTESA1genetic
20810648
GCN5_YEASTGCN5physical
20810648
HOSM_YEASTLYS21genetic
20810648
H4_YEASTHHF1physical
20810648
HOSC_YEASTLYS20physical
22615397
ASK10_YEASTASK10genetic
27708008
GAS1_YEASTGAS1genetic
27708008
CCZ1_YEASTCCZ1genetic
27708008
SSH1_YEASTSSH1genetic
27708008
STE50_YEASTSTE50genetic
27708008
MGR1_YEASTMGR1genetic
27708008
RIM1_YEASTRIM1genetic
27708008
THRC_YEASTTHR4genetic
27708008
IMG2_YEASTIMG2genetic
27708008
GCN20_YEASTGCN20genetic
27708008
GCN1_YEASTGCN1genetic
27708008
ARO8_YEASTARO8genetic
27708008
RTF1_YEASTRTF1genetic
27708008
SDS3_YEASTSDS3genetic
27708008
ESL1_YEASTESL1genetic
27708008
PTK2_YEASTPTK2genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
SIC1_YEASTSIC1genetic
27708008
STM1_YEASTSTM1genetic
27708008
PFD6_YEASTYKE2genetic
27708008
TSA1_YEASTTSA1genetic
27708008
MAC1_YEASTMAC1genetic
27708008
MSS1_YEASTMSS1genetic
27708008
PALI_YEASTRIM9genetic
27708008
YHM2_YEASTYHM2genetic
27708008
SCS7_YEASTSCS7genetic
27708008
AEP2_YEASTAEP2genetic
27708008
UBP15_YEASTUBP15genetic
27708008
PUB1_YEASTPUB1genetic
27708008
IDH1_YEASTIDH1genetic
27708008
COX5A_YEASTCOX5Agenetic
27708008
ODP2_YEASTLAT1genetic
27708008
MKS1_YEASTMKS1genetic
27708008
NST1_YEASTNST1genetic
27708008
RAS2_YEASTRAS2genetic
27708008
VPS27_YEASTVPS27genetic
27708008
IDH2_YEASTIDH2genetic
27708008
MSC6_YEASTMSC6genetic
27708008
COX10_YEASTCOX10genetic
27708008
RTC6_YEASTRTC6genetic
27708008
MDL2_YEASTMDL2genetic
27708008
YME1_YEASTYME1genetic
27708008
MSS18_YEASTMSS18genetic
27708008
VPS4_YEASTVPS4genetic
27708008
ARP8_YEASTARP8genetic
25628362
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HOSC_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-395; THR-396; SER-401AND SER-410, 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 THR-396 AND SER-410, ANDMASS 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-395; THR-396 ANDSER-401, AND MASS 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 THR-396, 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-396, AND MASSSPECTROMETRY.

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