HMDH1_YEAST - dbPTM
HMDH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HMDH1_YEAST
UniProt AC P12683
Protein Name 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1
Gene Name HMG1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1054
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein. Nucleus envelope.
Protein Description One of 2 isozymes that catalyze the conversion of HMG-CoA to mevalonate. It is the rate-limiting enzyme of the sterol biosynthesis pathway. Involved in ergosterol biosynthesis..
Protein Sequence MPPLFKGLKQMAKPIAYVSRFSAKRPIHIILFSLIISAFAYLSVIQYYFNGWQLDSNSVFETAPNKDSNTLFQECSHYYRDSSLDGWVSITAHEASELPAPHHYYLLNLNFNSPNETDSIPELANTVFEKDNTKYILQEDLSVSKEISSTDGTKWRLRSDRKSLFDVKTLAYSLYDVFSENVTQADPFDVLIMVTAYLMMFYTIFGLFNDMRKTGSNFWLSASTVVNSASSLFLALYVTQCILGKEVSALTLFEGLPFIVVVVGFKHKIKIAQYALEKFERVGLSKRITTDEIVFESVSEEGGRLIQDHLLCIFAFIGCSMYAHQLKTLTNFCILSAFILIFELILTPTFYSAILALRLEMNVIHRSTIIKQTLEEDGVVPSTARIISKAEKKSVSSFLNLSVVVIIMKLSVILLFVFINFYNFGANWVNDAFNSLYFDKERVSLPDFITSNASENFKEQAIVSVTPLLYYKPIKSYQRIEDMVLLLLRNVSVAIRDRFVSKLVLSALVCSAVINVYLLNAARIHTSYTADQLVKTEVTKKSFTAPVQKASTPVLTNKTVISGSKVKSLSSAQSSSSGPSSSSEEDDSRDIESLDKKIRPLEELEALLSSGNTKQLKNKEVAALVIHGKLPLYALEKKLGDTTRAVAVRRKALSILAEAPVLASDRLPYKNYDYDRVFGACCENVIGYMPLPVGVIGPLVIDGTSYHIPMATTEGCLVASAMRGCKAINAGGGATTVLTKDGMTRGPVVRFPTLKRSGACKIWLDSEEGQNAIKKAFNSTSRFARLQHIQTCLAGDLLFMRFRTTTGDAMGMNMISKGVEYSLKQMVEEYGWEDMEVVSVSGNYCTDKKPAAINWIEGRGKSVVAEATIPGDVVRKVLKSDVSALVELNIAKNLVGSAMAGSVGGFNAHAANLVTAVFLALGQDPAQNVESSNCITLMKEVDGDLRISVSMPSIEVGTIGGGTVLEPQGAMLDLLGVRGPHATAPGTNARQLARIVACAVLAGELSLCAALAAGHLVQSHMTHNRKPAEPTKPNNLDATDINRLKDGSVTCIKS
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
115N-linked_GlycosylationNLNFNSPNETDSIPE
ECCCCCCCCCCCCHH		65.70-
181N-linked_GlycosylationLYDVFSENVTQADPF
HHHHHCCCCCCCCHH		40.72-
452N-linked_GlycosylationLPDFITSNASENFKE
CCHHHCCCCCCCHHH		38.54-
464PhosphorylationFKEQAIVSVTPLLYY
HHHHEEEEECHHEEC		17.7326447709
466PhosphorylationEQAIVSVTPLLYYKP
HHEEEEECHHEECCC		10.7426447709
470PhosphorylationVSVTPLLYYKPIKSY
EEECHHEECCCCCCC		19.6826447709
471PhosphorylationSVTPLLYYKPIKSYQ
EECHHEECCCCCCCC		15.4026447709
490N-linked_GlycosylationMVLLLLRNVSVAIRD
HHHHHHHHHCHHHHH		30.31-
542PhosphorylationKTEVTKKSFTAPVQK
EEEECCCEECCCCCC		29.4127717283
544PhosphorylationEVTKKSFTAPVQKAS
EECCCEECCCCCCCC		36.8227717283
551PhosphorylationTAPVQKASTPVLTNK
CCCCCCCCCCCCCCC		40.0429136822
552PhosphorylationAPVQKASTPVLTNKT
CCCCCCCCCCCCCCE		23.4417330950
556PhosphorylationKASTPVLTNKTVISG
CCCCCCCCCCEEECC		34.6029136822
568PhosphorylationISGSKVKSLSSAQSS
ECCCCEEECCCCCCC		36.1523749301
570PhosphorylationGSKVKSLSSAQSSSS
CCCEEECCCCCCCCC		30.6223749301
571PhosphorylationSKVKSLSSAQSSSSG
CCEEECCCCCCCCCC		35.3022369663
574PhosphorylationKSLSSAQSSSSGPSS
EECCCCCCCCCCCCC		31.7222369663
575PhosphorylationSLSSAQSSSSGPSSS
ECCCCCCCCCCCCCC		19.2222369663
576PhosphorylationLSSAQSSSSGPSSSS
CCCCCCCCCCCCCCC		44.5622369663
577PhosphorylationSSAQSSSSGPSSSSE
CCCCCCCCCCCCCCC		57.5822369663
580PhosphorylationQSSSSGPSSSSEEDD
CCCCCCCCCCCCCCC		46.5122369663
581PhosphorylationSSSSGPSSSSEEDDS
CCCCCCCCCCCCCCC		40.8022369663
582PhosphorylationSSSGPSSSSEEDDSR
CCCCCCCCCCCCCCC		46.2122369663
583PhosphorylationSSGPSSSSEEDDSRD
CCCCCCCCCCCCCCC		47.1322369663
588PhosphorylationSSSEEDDSRDIESLD
CCCCCCCCCCHHHHH		44.1422369663
593PhosphorylationDDSRDIESLDKKIRP
CCCCCHHHHHHHCCH		42.0522369663
596AcetylationRDIESLDKKIRPLEE
CCHHHHHHHCCHHHH		56.2324489116
597UbiquitinationDIESLDKKIRPLEEL
CHHHHHHHCCHHHHH		43.5517644757
609PhosphorylationEELEALLSSGNTKQL
HHHHHHHHCCCCHHH		36.7328889911
614UbiquitinationLLSSGNTKQLKNKEV
HHHCCCCHHHCCHHH		58.6017644757
619AcetylationNTKQLKNKEVAALVI
CCHHHCCHHHHHHEE		52.5624489116
637AcetylationLPLYALEKKLGDTTR
CHHHHHHHHHCCCHH		54.9024489116
651UbiquitinationRAVAVRRKALSILAE
HHHHHHHHHHHHHHC		43.0217644757
651AcetylationRAVAVRRKALSILAE
HHHHHHHHHHHHHHC		43.0224489116
670UbiquitinationASDRLPYKNYDYDRV
CCCCCCCCCCCHHHH		47.2817644757
726UbiquitinationASAMRGCKAINAGGG
HHHHHCCCEEECCCC		55.9423749301
726AcetylationASAMRGCKAINAGGG
HHHHHCCCEEECCCC		55.9424489116
740AcetylationGATTVLTKDGMTRGP
CCEEEECCCCCCCCC		48.3922865919
740UbiquitinationGATTVLTKDGMTRGP
CCEEEECCCCCCCCC		48.3924961812
817AcetylationMGMNMISKGVEYSLK
HHHHHHHCCCCHHHH		56.9322865919
848UbiquitinationSGNYCTDKKPAAINW
ECCCCCCCCCCCCEE		42.3717644757
849UbiquitinationGNYCTDKKPAAINWI
CCCCCCCCCCCCEEE		42.5717644757
1048PhosphorylationINRLKDGSVTCIKS-
HHCCCCCCEEEECC-		25.1223749301
1054PhosphorylationGSVTCIKS-------
CCEEEECC-------		26.0823749301
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
-KUbiquitinationE3 ubiquitin ligaseHRD1Q08109
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HMDH1_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 HMDH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HRD1_YEASTHRD1physical
11390656
RAD51_YEASTRAD51physical
16429126
RL27A_YEASTRPL27Aphysical
16429126
HMDH2_YEASTHMG2genetic
16269340
ATC6_YEASTSPF1genetic
16269340
SCS7_YEASTSCS7genetic
16269340
GSF2_YEASTGSF2genetic
16269340
PAN1_YEASTPAN1genetic
16269340
GPT2_YEASTGPT2genetic
16269340
BRE4_YEASTBRE4genetic
16269340
RGP1_YEASTRGP1genetic
16269340
RIC1_YEASTRIC1genetic
16269340
GGPPS_YEASTBTS1genetic
19592534
FPPS_YEASTERG20genetic
19592534
DPP1_YEASTDPP1genetic
19592534
HMDH2_YEASTHMG2genetic
18408719
HMDH2_YEASTHMG2genetic
16941010
PUR7_YEASTADE1genetic
20093466
UIP3_YEASTUIP3genetic
20093466
OSH1_YEASTSWH1genetic
20093466
SEA4_YEASTSEA4genetic
20093466
TREB_YEASTNTH2genetic
20093466
PYC2_YEASTPYC2genetic
20093466
PHO2_YEASTPHO2genetic
20093466
BSC2_YEASTBSC2genetic
20093466
YFH7_YEASTYFH7genetic
20093466
RMD8_YEASTRMD8genetic
20093466
SUT1_YEASTSUT1genetic
20093466
YG036_YEASTYGL036Wgenetic
20093466
RPN14_YEASTRPN14genetic
20093466
KEL2_YEASTKEL2genetic
20093466
SODM_YEASTSOD2genetic
20093466
YHI2_YEASTYHR022Cgenetic
20093466
HOS4_YEASTHOS4genetic
20093466
RGI2_YEASTRGI2genetic
20093466
RS21B_YEASTRPS21Bgenetic
20093466
IME1_YEASTIME1genetic
20093466
SEG2_YEASTSEG2genetic
20093466
DAL80_YEASTDAL80genetic
20093466
YL036_YEASTYLR036Cgenetic
20093466
RSSA2_YEASTRPS0Bgenetic
20093466
HMDH2_YEASTHMG2genetic
20093466
BCH1_YEASTBCH1genetic
20093466
SCS7_YEASTSCS7genetic
20093466
FKBP_YEASTFPR1genetic
20093466
RS7B_YEASTRPS7Bgenetic
20093466
RU2A_YEASTLEA1genetic
20093466
AIM44_YEASTAIM44genetic
20093466
GGPPS_YEASTBTS1genetic
20093466
BRR1_YEASTBRR1genetic
20093466
MDM36_YEASTMDM36genetic
20093466
YP098_YEASTYPR098Cgenetic
20093466
YP153_YEASTYPR153Wgenetic
20093466
MLC2_YEASTMLC2genetic
20093466
SKI3_YEASTSKI3genetic
20093466
PHO88_YEASTPHO88physical
16093310
MKAR_YEASTIFA38physical
16093310
IRE1_YEASTIRE1physical
16093310
SNL1_YEASTSNL1physical
16093310
SRPB_YEASTSRP102physical
16093310
SPO75_YEASTSPO75physical
16093310
ELO3_YEASTELO3physical
16093310
HMDH1_YEASTHMG1physical
16093310
UTH1_YEASTUTH1genetic
19325107
VPS52_YEASTVPS52genetic
19325107
VPS53_YEASTVPS53genetic
19325107
BRE5_YEASTBRE5genetic
19325107
GGPPS_YEASTBTS1genetic
19325107
ISW2_YEASTISW2genetic
19325107
SSH1_YEASTSSH1genetic
19325107
HMDH2_YEASTHMG2genetic
3526336
HMDH2_YEASTHMG2genetic
21623372
GGPPS_YEASTBTS1genetic
21623372
CSG2_YEASTCSG2genetic
21623372
ERG2_YEASTERG2genetic
21623372
FDFT_YEASTERG9genetic
26614300
ECM33_YEASTECM33genetic
27708008
YL036_YEASTYLR036Cgenetic
27708008
ARE1_YEASTARE1genetic
27708008
PHO2_YEASTPHO2genetic
27708008
PAA1_YEASTPAA1genetic
27708008
RRP8_YEASTRRP8genetic
27708008
SWI5_YEASTSWI5genetic
27708008
SNF1_YEASTSNF1genetic
27708008
RAD4_YEASTRAD4genetic
27708008
FAB1_YEASTFAB1genetic
27708008
RMD8_YEASTRMD8genetic
27708008
RT31_YEASTYMR31genetic
27708008
YG036_YEASTYGL036Wgenetic
27708008
SLX9_YEASTSLX9genetic
27708008
YHI2_YEASTYHR022Cgenetic
27708008
YIF4_YEASTYIL054Wgenetic
27708008
BMT5_YEASTBMT5genetic
27708008
SIP4_YEASTSIP4genetic
27708008
ELO1_YEASTELO1genetic
27708008
IME1_YEASTIME1genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
SEG2_YEASTSEG2genetic
27708008
YKR18_YEASTYKR018Cgenetic
27708008
DAL80_YEASTDAL80genetic
27708008
AVL9_YEASTAVL9genetic
27708008
ARV1_YEASTARV1genetic
27708008
RS29A_YEASTRPS29Agenetic
27708008
HMDH2_YEASTHMG2genetic
27708008
MSS1_YEASTMSS1genetic
27708008
COX7_YEASTCOX7genetic
27708008
SCS7_YEASTSCS7genetic
27708008
YN87_YEASTYNR014Wgenetic
27708008
ULS1_YEASTULS1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
RLM1_YEASTRLM1genetic
27708008
RU2A_YEASTLEA1genetic
27708008
UBA3_YEASTUBA3genetic
27708008
MDM36_YEASTMDM36genetic
27708008
YP153_YEASTYPR153Wgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HMDH1_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-552 AND SER-609, ANDMASS 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-580 AND SER-581, 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 THR-552, AND MASSSPECTROMETRY.

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