HMCS_YEAST - dbPTM
HMCS_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HMCS_YEAST
UniProt AC P54839
Protein Name Hydroxymethylglutaryl-CoA synthase
Gene Name ERG13
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 491
Subcellular Localization
Protein Description This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase..
Protein Sequence MKLSTKLCWCGIKGRLRPQKQQQLHNTNLQMTELKKQKTAEQKTRPQNVGIKGIQIYIPTQCVNQSELEKFDGVSQGKYTIGLGQTNMSFVNDREDIYSMSLTVLSKLIKSYNIDTNKIGRLEVGTETLIDKSKSVKSVLMQLFGENTDVEGIDTLNACYGGTNALFNSLNWIESNAWDGRDAIVVCGDIAIYDKGAARPTGGAGTVAMWIGPDAPIVFDSVRASYMEHAYDFYKPDFTSEYPYVDGHFSLTCYVKALDQVYKSYSKKAISKGLVSDPAGSDALNVLKYFDYNVFHVPTCKLVTKSYGRLLYNDFRANPQLFPEVDAELATRDYDESLTDKNIEKTFVNVAKPFHKERVAQSLIVPTNTGNMYTASVYAAFASLLNYVGSDDLQGKRVGLFSYGSGLAASLYSCKIVGDVQHIIKELDITNKLAKRITETPKDYEAAIELRENAHLKKNFKPQGSIEHLQSGVYYLTNIDDKFRRSYDVKK
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
43AcetylationKQKTAEQKTRPQNVG
HHHCHHHHCCCCCCC		37.7022865919
70AcetylationVNQSELEKFDGVSQG
CCHHHHHCCCCCCCC		62.4724489116
75PhosphorylationLEKFDGVSQGKYTIG
HHCCCCCCCCCEEEE		38.4527717283
79PhosphorylationDGVSQGKYTIGLGQT
CCCCCCCEEEEECCC		15.4821440633
110AcetylationTVLSKLIKSYNIDTN
HHHHHHHHHCCCCCC		58.2724489116
110SuccinylationTVLSKLIKSYNIDTN
HHHHHHHHHCCCCCC		58.2723954790
118AcetylationSYNIDTNKIGRLEVG
HCCCCCCCCCCEECC		48.9424489116
118UbiquitinationSYNIDTNKIGRLEVG
HCCCCCCCCCCEECC		48.9423749301
126PhosphorylationIGRLEVGTETLIDKS
CCCEECCCCHHHCCC		30.8522369663
128PhosphorylationRLEVGTETLIDKSKS
CEECCCCHHHCCCCC		28.9322369663
132AcetylationGTETLIDKSKSVKSV
CCCHHHCCCCCHHHH		53.4424489116
1322-HydroxyisobutyrylationGTETLIDKSKSVKSV
CCCHHHCCCCCHHHH		53.44-
133PhosphorylationTETLIDKSKSVKSVL
CCHHHCCCCCHHHHH		26.8128889911
135PhosphorylationTLIDKSKSVKSVLMQ
HHHCCCCCHHHHHHH		41.7028889911
2632-HydroxyisobutyrylationKALDQVYKSYSKKAI
HHHHHHHHHCCCHHH		44.02-
263AcetylationKALDQVYKSYSKKAI
HHHHHHHHHCCCHHH		44.0224489116
263SuccinylationKALDQVYKSYSKKAI
HHHHHHHHHCCCHHH		44.0223954790
263UbiquitinationKALDQVYKSYSKKAI
HHHHHHHHHCCCHHH		44.0223749301
267UbiquitinationQVYKSYSKKAISKGL
HHHHHCCCHHHHCCC		37.6822817900
268UbiquitinationVYKSYSKKAISKGLV
HHHHCCCHHHHCCCC		45.0422817900
272UbiquitinationYSKKAISKGLVSDPA
CCCHHHHCCCCCCCC		50.5823749301
276PhosphorylationAISKGLVSDPAGSDA
HHHCCCCCCCCCCCH		42.8122369663
281PhosphorylationLVSDPAGSDALNVLK
CCCCCCCCCHHHHHH		23.0922369663
288UbiquitinationSDALNVLKYFDYNVF
CCHHHHHHHCCCCEE		39.3217644757
301UbiquitinationVFHVPTCKLVTKSYG
EECCCCHHEEECCCC		48.7723749301
301AcetylationVFHVPTCKLVTKSYG
EECCCCHHEEECCCC		48.7724489116
305AcetylationPTCKLVTKSYGRLLY
CCHHEEECCCCHHHH		33.9122865919
3052-HydroxyisobutyrylationPTCKLVTKSYGRLLY
CCHHEEECCCCHHHH		33.91-
305UbiquitinationPTCKLVTKSYGRLLY
CCHHEEECCCCHHHH		33.9123749301
3412-HydroxyisobutyrylationYDESLTDKNIEKTFV
CCCCCCCCCHHHHCC		55.37-
341AcetylationYDESLTDKNIEKTFV
CCCCCCCCCHHHHCC		55.3724489116
345AcetylationLTDKNIEKTFVNVAK
CCCCCHHHHCCCCCC		43.3924489116
352AcetylationKTFVNVAKPFHKERV
HHCCCCCCCCCHHHH		43.8924489116
356AcetylationNVAKPFHKERVAQSL
CCCCCCCHHHHCCEE		47.8224489116
415UbiquitinationAASLYSCKIVGDVQH
HHHHHHCEEHHCHHH		34.1917644757
425UbiquitinationGDVQHIIKELDITNK
HCHHHHHHHCCCHHH		52.1817644757
425AcetylationGDVQHIIKELDITNK
HCHHHHHHHCCCHHH		52.1824489116
432UbiquitinationKELDITNKLAKRITE
HHCCCHHHHHHHHHC		40.9717644757
432AcetylationKELDITNKLAKRITE
HHCCCHHHHHHHHHC		40.9724489116
438PhosphorylationNKLAKRITETPKDYE
HHHHHHHHCCCCCHH		37.5328889911
442AcetylationKRITETPKDYEAAIE
HHHHCCCCCHHHHHH		79.1124489116
457SuccinylationLRENAHLKKNFKPQG
HHHHHHHCCCCCCCC		35.4923954790
458UbiquitinationRENAHLKKNFKPQGS
HHHHHHCCCCCCCCC		74.1717644757
461UbiquitinationAHLKKNFKPQGSIEH
HHHCCCCCCCCCHHH		45.9122106047
461AcetylationAHLKKNFKPQGSIEH
HHHCCCCCCCCCHHH		45.9124489116
465PhosphorylationKNFKPQGSIEHLQSG
CCCCCCCCHHHHCCC		21.4021551504
474PhosphorylationEHLQSGVYYLTNIDD
HHHCCCEEEEECCCH		9.0421551504
482AcetylationYLTNIDDKFRRSYDV
EEECCCHHHHHHCCC		36.7024489116
482UbiquitinationYLTNIDDKFRRSYDV
EEECCCHHHHHHCCC		36.7017644757
486PhosphorylationIDDKFRRSYDVKK--
CCHHHHHHCCCCC--		22.7921551504
487PhosphorylationDDKFRRSYDVKK---
CHHHHHHCCCCC---		23.9721551504
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 HMCS_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HMCS_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 HMCS_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACT_YEASTACT1physical
11805826
LYS12_YEASTLYS12physical
11805826
RRN3_YEASTRRN3physical
11805826
METK1_YEASTSAM1physical
11805826
CTU2_YEASTNCS2physical
11805826
BUL1_YEASTBUL1genetic
12810702
THRC_YEASTTHR4physical
16554755
RL13B_YEASTRPL13Bphysical
16429126
RL17A_YEASTRPL17Aphysical
16429126
RL24A_YEASTRPL24Aphysical
16429126
RL25_YEASTRPL25physical
16429126
RL30_YEASTRPL30physical
16429126
RL35A_YEASTRPL35Aphysical
16429126
RL35B_YEASTRPL35Aphysical
16429126
RL7A_YEASTRPL7Aphysical
16429126
RS22A_YEASTRPS22Aphysical
16429126
RS24A_YEASTRPS24Bphysical
16429126
RS24B_YEASTRPS24Bphysical
16429126
RS25A_YEASTRPS25Aphysical
16429126
RRN3_YEASTRRN3physical
16429126
GGPPS_YEASTBTS1genetic
21623372
ERG2_YEASTERG2genetic
21623372
AATC_YEASTAAT2genetic
21623372
CSG2_YEASTCSG2genetic
21623372
LCB5_YEASTLCB5genetic
21623372
MET22_YEASTMET22genetic
21623372
THRC_YEASTTHR4genetic
21623372
TAL1_YEASTTAL1genetic
21623372
SUR1_YEASTSUR1genetic
21623372
KAD2_YEASTADK1genetic
21623372
SYSM_YEASTDIA4genetic
21623372
FUMH_YEASTFUM1genetic
21623372
SCS7_YEASTSCS7genetic
21623372
METC_YEASTIRC7genetic
21623372
DHOM_YEASTHOM6genetic
21623372
CSG2_YEASTCSG2genetic
23891562
ICE2_YEASTICE2genetic
23891562
RPN5_YEASTRPN5genetic
27708008
ERF3_YEASTSUP35genetic
27708008
SAD1_YEASTSAD1genetic
27708008
FDFT_YEASTERG9genetic
27708008
MNN11_YEASTMNN11genetic
27708008
ACE2_YEASTACE2genetic
27708008
SRO7_YEASTSRO7genetic
27708008
AXL1_YEASTAXL1genetic
27708008
KPC1_YEASTPKC1genetic
27708008
GPI18_YEASTGPI18genetic
27708008
ALG14_YEASTALG14genetic
27708008
CALM_YEASTCMD1genetic
27708008
MCM7_YEASTMCM7genetic
27708008
RPB1_YEASTRPO21genetic
27708008
TCPD_YEASTCCT4genetic
27708008
UPPS_YEASTNUS1genetic
27708008
RRP1_YEASTRRP1genetic
27708008
TAF12_YEASTTAF12genetic
27708008
SLY1_YEASTSLY1genetic
27708008
CAB5_YEASTCAB5genetic
27708008
TCPA_YEASTTCP1genetic
27708008
RIFK_YEASTFMN1genetic
27708008
GPI11_YEASTGPI11genetic
27708008
GPI8_YEASTGPI8genetic
27708008
NCS1_YEASTFRQ1genetic
27708008
GPI19_YEASTGPI19genetic
27708008
SEC20_YEASTSEC20genetic
27708008
PANK_YEASTCAB1genetic
27708008
TSC11_YEASTTSC11genetic
27708008
GDI1_YEASTGDI1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
STT3_YEASTSTT3genetic
27708008
NBP35_YEASTNBP35genetic
27708008
GPI10_YEASTGPI10genetic
27708008
PGTB1_YEASTCDC43genetic
27708008
SEC15_YEASTSEC15genetic
27708008
BRR6_YEASTBRR6genetic
27708008
SMD1_YEASTSMD1genetic
27708008
ZPR1_YEASTZPR1genetic
27708008
BRL1_YEASTBRL1genetic
27708008
RRP4_YEASTRRP4genetic
27708008
RPF1_YEASTRPF1genetic
27708008
GPI16_YEASTGPI16genetic
27708008
ATC7_YEASTNEO1genetic
27708008
RHO3_YEASTRHO3genetic
27708008
ARP4_YEASTARP4genetic
27708008
EXO70_YEASTEXO70genetic
27708008
TIM16_YEASTPAM16genetic
27708008
YJ9I_YEASTYJR141Wgenetic
27708008
SN114_YEASTSNU114genetic
27708008
YKT6_YEASTYKT6genetic
27708008
BET3_YEASTBET3genetic
27708008
RPF2_YEASTRPF2genetic
27708008
SSL1_YEASTSSL1genetic
27708008
BOS1_YEASTBOS1genetic
27708008
ERG27_YEASTERG27genetic
27708008
SEC22_YEASTSEC22genetic
27708008
TAF7_YEASTTAF7genetic
27708008
GPI12_YEASTGPI12genetic
27708008
DCP2_YEASTDCP2genetic
27708008
CAP_YEASTSRV2genetic
27708008
DBP6_YEASTDBP6genetic
27708008
HRP1_YEASTHRP1genetic
27708008
TYSY_YEASTCDC21genetic
27708008
RPB2_YEASTRPB2genetic
27708008
GPI2_YEASTGPI2genetic
27708008
MOT1_YEASTMOT1genetic
27708008
TBF1_YEASTTBF1genetic
27708008
NAB3_YEASTNAB3genetic
27708008
TF2B_YEASTSUA7genetic
27708008
SRP54_YEASTSRP54genetic
27708008
MED10_YEASTNUT2genetic
27708008
PGTB2_YEASTBET2genetic
27708008
SEC23_YEASTSEC23genetic
27708008
DPM1_YEASTDPM1genetic
27708008
ATC3_YEASTDRS2genetic
27708008
RS8A_YEASTRPS8Agenetic
27708008
RS8B_YEASTRPS8Agenetic
27708008
PAT1_YEASTPAT1genetic
27708008
GET3_YEASTGET3genetic
27708008
GET1_YEASTGET1genetic
27708008
PALF_YEASTRIM8genetic
27708008
CHO2_YEASTCHO2genetic
27708008
SLT2_YEASTSLT2genetic
27708008
VPS53_YEASTVPS53genetic
27708008
BCK1_YEASTBCK1genetic
27708008
LSM1_YEASTLSM1genetic
27708008
VPS55_YEASTVPS55genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
CTK1_YEASTCTK1genetic
27708008
CANB_YEASTCNB1genetic
27708008
DBP7_YEASTDBP7genetic
27708008
ENT4_YEASTENT4genetic
27708008
CSF1_YEASTCSF1genetic
27708008
ARV1_YEASTARV1genetic
27708008
CDC73_YEASTCDC73genetic
27708008
RIM13_YEASTRIM13genetic
27708008
RS10B_YEASTRPS10Bgenetic
27708008
RNH1_YEASTRNH1genetic
27708008
TOP1_YEASTTOP1genetic
27708008
GYP1_YEASTGYP1genetic
27708008
FYV12_YEASTFYV12genetic
27708008
SUR1_YEASTSUR1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
AIM44_YEASTAIM44genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HMCS_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-276, AND MASSSPECTROMETRY.

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