ERG27_YEAST - dbPTM
ERG27_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERG27_YEAST
UniProt AC Q12452
Protein Name 3-keto-steroid reductase
Gene Name ERG27
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 347
Subcellular Localization Endoplasmic reticulum membrane
Peripheral membrane protein. Lipid droplet.
Protein Description Responsible for the reduction of the keto group on the C-3 of sterols. Also facilitates the association of ERG7 with lipid particles preventing its digestion in the endoplasmic reticulum and the lipid particles..
Protein Sequence MNRKVAIVTGTNSNLGLNIVFRLIETEDTNVRLTIVVTSRTLPRVQEVINQIKDFYNKSGRVEDLEIDFDYLLVDFTNMVSVLNAYYDINKKYRAINYLFVNAAQGIFDGIDWIGAVKEVFTNPLEAVTNPTYKIQLVGVKSKDDMGLIFQANVFGPYYFISKILPQLTRGKAYIVWISSIMSDPKYLSLNDIELLKTNASYEGSKRLVDLLHLATYKDLKKLGINQYVVQPGIFTSHSFSEYLNFFTYFGMLCLFYLARLLGSPWHNIDGYKAANAPVYVTRLANPNFEKQDVKYGSATSRDGMPYIKTQEIDPTGMSDVFAYIQKKKLEWDEKLKDQIVETRTPI
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
4Ubiquitination----MNRKVAIVTGT
----CCCEEEEEECC		30.8917644757
53UbiquitinationQEVINQIKDFYNKSG
HHHHHHHHHHHHHCC		31.8324961812
53AcetylationQEVINQIKDFYNKSG
HHHHHHHHHHHHHCC		31.8324489116
58UbiquitinationQIKDFYNKSGRVEDL
HHHHHHHHCCCCEEE		42.8022817900
118UbiquitinationIDWIGAVKEVFTNPL
CCHHHHHHHHHCCCH		47.8517644757
134UbiquitinationAVTNPTYKIQLVGVK
HHCCCCEEEEEEECC		26.8423749301
141UbiquitinationKIQLVGVKSKDDMGL
EEEEEECCCCCCCEE		45.9517644757
197AcetylationLNDIELLKTNASYEG
HHHHHHHHHCCCCCH		52.9724489116
218AcetylationLLHLATYKDLKKLGI
HHHHHHHHHHHHHCC		52.8324489116
218UbiquitinationLLHLATYKDLKKLGI
HHHHHHHHHHHHHCC		52.8317644757
221AcetylationLATYKDLKKLGINQY
HHHHHHHHHHCCCEE		56.9624489116
221UbiquitinationLATYKDLKKLGINQY
HHHHHHHHHHCCCEE		56.9617644757
222UbiquitinationATYKDLKKLGINQYV
HHHHHHHHHCCCEEE		60.2817644757
273UbiquitinationWHNIDGYKAANAPVY
CCCCCCHHHCCCCEE		46.6917644757
291UbiquitinationLANPNFEKQDVKYGS
CCCCCCCCCCCCCCC		47.8923749301
291AcetylationLANPNFEKQDVKYGS
CCCCCCCCCCCCCCC		47.8924489116
295UbiquitinationNFEKQDVKYGSATSR
CCCCCCCCCCCCCCC		52.7823749301
295AcetylationNFEKQDVKYGSATSR
CCCCCCCCCCCCCCC		52.7824489116
309UbiquitinationRDGMPYIKTQEIDPT
CCCCCCEEEEECCCC		38.0123749301
327AcetylationDVFAYIQKKKLEWDE
HHHHHHHHHCCCCCH		42.1724489116
328UbiquitinationVFAYIQKKKLEWDEK
HHHHHHHHCCCCCHH		46.3317644757
329UbiquitinationFAYIQKKKLEWDEKL
HHHHHHHCCCCCHHH		59.6917644757
335UbiquitinationKKLEWDEKLKDQIVE
HCCCCCHHHHHHHHH		59.3617644757
337UbiquitinationLEWDEKLKDQIVETR
CCCCHHHHHHHHHCC		59.6723749301
343PhosphorylationLKDQIVETRTPI---
HHHHHHHCCCCC---		29.0228889911
345PhosphorylationDQIVETRTPI-----
HHHHHCCCCC-----		32.5225521595
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 ERG27_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERG27_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 ERG27_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERG7_YEASTERG7physical
12842197
ERG28_YEASTERG28physical
12119386
ENG2_YEASTACF2physical
18467557
ERG3_YEASTERG3physical
16300994
ERG6_YEASTERG6physical
16300994
ERG28_YEASTERG28physical
16300994
ERG27_YEASTERG27physical
16300994
MSMO_YEASTERG25physical
16300994
ERG24_YEASTERG24physical
16300994
CP51_YEASTERG11physical
16300994
ERG7_YEASTERG7physical
16300994
SEC7_YEASTSEC7genetic
23891562
SLX5_YEASTSLX5genetic
27708008
VPS41_YEASTVPS41genetic
27708008
VPS4_YEASTVPS4genetic
27708008
KPC1_YEASTPKC1genetic
27708008
CALM_YEASTCMD1genetic
27708008
CKS1_YEASTCKS1genetic
27708008
CDC10_YEASTCDC10genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
CDC11_YEASTCDC11genetic
27708008
EI2BB_YEASTGCD7genetic
27708008
GSP1_YEASTGSP1genetic
27708008
RU1C_YEASTYHC1genetic
27708008
STT4_YEASTSTT4genetic
27708008
CDC25_YEASTCDC25genetic
27708008
CDC3_YEASTCDC3genetic
27708008
TAD3_YEASTTAD3genetic
27708008
RLA0_YEASTRPP0genetic
27708008
IMB1_YEASTKAP95genetic
27708008
RNA1_YEASTRNA1genetic
27708008
PROF_YEASTPFY1genetic
27708008
DYR_YEASTDFR1genetic
27708008
MYO2_YEASTMYO2genetic
27708008
MOT1_YEASTMOT1genetic
27708008
DEP1_YEASTDEP1genetic
27708008
FUN26_YEASTFUN26genetic
27708008
SWD1_YEASTSWD1genetic
27708008
GPT1_YEASTSCT1genetic
27708008
NCL1_YEASTNCL1genetic
27708008
PIN4_YEASTPIN4genetic
27708008
MNN2_YEASTMNN2genetic
27708008
GAL10_YEASTGAL10genetic
27708008
FAT1_YEASTFAT1genetic
27708008
SWC5_YEASTSWC5genetic
27708008
SGF29_YEASTSGF29genetic
27708008
AGP1_YEASTAGP1genetic
27708008
FIG2_YEASTFIG2genetic
27708008
HBT1_YEASTHBT1genetic
27708008
ARO1_YEASTARO1genetic
27708008
UPC2_YEASTUPC2genetic
27708008
MNN10_YEASTMNN10genetic
27708008
ERD1_YEASTERD1genetic
27708008
DOT1_YEASTDOT1genetic
27708008
PEA2_YEASTPEA2genetic
27708008
FAR7_YEASTFAR7genetic
27708008
SGF73_YEASTSGF73genetic
27708008
YGI1_YEASTYGL081Wgenetic
27708008
YGZ2_YEASTYGL242Cgenetic
27708008
PEX31_YEASTPEX31genetic
27708008
HGH1_YEASTHGH1genetic
27708008
CCH1_YEASTCCH1genetic
27708008
TNA1_YEASTTNA1genetic
27708008
OPI1_YEASTOPI1genetic
27708008
SLT2_YEASTSLT2genetic
27708008
MTC6_YEASTMTC6genetic
27708008
URM1_YEASTURM1genetic
27708008
BCK1_YEASTBCK1genetic
27708008
HOC1_YEASTHOC1genetic
27708008
CANB_YEASTCNB1genetic
27708008
TRPG_YEASTTRP3genetic
27708008
MID2_YEASTMID2genetic
27708008
SEI1_YEASTFLD1genetic
27708008
CDC73_YEASTCDC73genetic
27708008
TSA1_YEASTTSA1genetic
27708008
HMDH1_YEASTHMG1genetic
27708008
AIM34_YEASTAIM34genetic
27708008
GBLP_YEASTASC1genetic
27708008
CRZ1_YEASTCRZ1genetic
27708008
CTU2_YEASTNCS2genetic
27708008
SIN3_YEASTSIN3genetic
27708008
ALG6_YEASTALG6genetic
27708008
COQ7_YEASTCAT5genetic
27708008
NPT1_YEASTNPT1genetic
27708008
ENV9_YEASTENV9genetic
27708008
MRX11_YEASTYPL041Cgenetic
27708008
LGE1_YEASTLGE1genetic
27708008
SUR1_YEASTSUR1genetic
27708008
PRM3_YEASTPRM3genetic
27708008
CG12_YEASTCLN2genetic
27708008
YP272_YEASTPBI1genetic
27708008
CSR2_YEASTCSR2genetic
27708008
CHMU_YEASTARO7genetic
27708008
SYT1_YEASTSYT1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERG27_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-345, AND MASSSPECTROMETRY.
"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-345, AND MASSSPECTROMETRY.

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